FORM 2 THE PATENTS ACT, 1970 (39 of 1970) & The Patent Rules, 2003 COMPLETE SPECIFICATION 1. TITLE OF THE INVENTION: ANGIOPOIETIN DERIVED PEPTIDES 2. APPLICANT: Name: COMPUGEN LTD. Nationality: Israel Address: 72 Pinchas Rosen Street, 69512 Tel Aviv, Israel. 3. PREAMBLE TO THE DESCRIPTION: The following specification particularly describes the invention and the manner in which it is to be performed:' FIELD OF THE INVENTION This invention relates to the field of angiogenesis related pathology. BACKGROUND OF THE INVENTION Angiogenesis, the process of new blood-vessel growth, plays an essential role in many physiological and pathological processes. It is a multi-step process including endothelial cell activation, proliferation, migration, penetration of extracellular matrix, reorganization of ceils into tubules, formation of a lumen, and anastomosis. Typically, angiogenesis is tightly regulated by pro- and anti-angiogenic factors and is crucial for development, reproduction and repair. Vasculogenesis and angiogenesis are down-regulated in the healthy adult and are - except for the organs of the female reproductive system - almost exclusively associated with pathology when angiogenesis is induced by microenvironmental factors (e.g. hypoxia or inflammation). Pathological processes associated with, or induced by, angiogenesis include diseases as diverse as cancer, and inflammatory disorders such as rheumatoid or rheumatic inflammatory disease, especially arthritis (including rheumatoid arthritis), or other chronic inflammatory disorders, such as chronic asthma, arterial or post-transplantational atherosclerosis, psoriasis, asthma, infections, obesity, diabetes, endometriosis, ocular neovascularisation, such as retinopathies (including diabetic retinopathy), macular degeneration, thrombosis, hemangioblastoma, and hemangioma (Folkman J., 2007 Nat Rev Drug Discov 6(4):273; Fiedler U. and Augustin EG, 2006 TRENDS Immun 27(12):552; Li L„ et al, 2005 Pediatr Endocrinol Rev. 2(3):399) Although a variety of factors can modulate endothelial cell (EC) responses in vitro, and blood vessel growth in vivo, only vascular endothelial growth factor (VEGF) family members and the angiopoietins are believed to act almost exclusively on vascular ECs. (Yancopoulos G., et al, 2000 Nature 407:242). The formation of functional vasculature is a complex process requiring spatial and temporal coordination of multiple angiogenic factors, receptors, intracellular signaling pathways and regulatory factors. Without being bound by theory, vascular endothelial growth factors (VEGFs) and angiopoietins (Angs) play complementary roles in this process. The Ang family comprises the ligands Angl, Ang2, Ang3, and Ang4. Their cognate Tie2/Tek receptor and a closely related orphan receptor, Tiel, are almost exclusively expressed by endothelial cells and hematopoietic stem cells. Tiel and Tie2 share a similar overall structure consisting of an extracellular domain and an intracellular tyrosine kinase domain. (Shim W.S.N., et al, 2007 Mol Cancer Res 5(7):655; Fiedler U. and Augustin EG., 2006 TRENDS Immun 27(12):552). The Angs contain an ammo-terminal angiopoietin specific domain, a coiled-coil domain, a linker peptide and a carboxy-terminal fibrinogen homology domain. The fibrinogen homology domain is responsible for receptor binding, the coiled-coil domain is required for dimerizafion of angiopoietin monomers, and the short amino-ferminaJ region forms ring-like structures that cluster dimers into variable sized multimers necessary for Tie2 activation. (EklundL andOlsenB.R, 2006 Exp Cell Res 312:630) Angl is known to form trimers and multimers to homodimerize and induce tyrosine phosphorylation of the Tie2 receptor for intracellular signaling. Dimeric form of Angl has been found to inactivate Tie2 receptor, and some isoforms of Angl have been reported to negatively regulate Tie2 activation (Shim W.S.N., et al, 2007 Mol Cancer Res 5(7):655). Angl binding to the extracellular domain of Tie2 results in receptor dimerization, allowing activation of the kinase domain and autophosphorylation of specific tyrosine residues, acting as docking sites for a number of effectors that couple the activated receptors to the cytoplasmic signaling pathways. Angl-stimulated Tie2 activation mediates remodeling and stabilization of cell-cell and cell-matrix interactions and plays a role in the recruitment of peri-endothelial mesenchymal cells to the vessels. In addition, Angl has anti-permeability and anti-inflammatory functions, and is also critically important in the formation of vascular networks during developmental angiogenesis (Ellund I. and Olsen BX 2006 Exp Cell Res 312:630; Shim W.S.N.,et al, 2007 Mol Cancer Res 5(7):655). Ang2 forms dimers to bind to Tie2, but does not induce autophosphorylation. In contrast to Angl, it is almost exclusively expressed by endothelial cells. Ang2 mRNA is almost undetectable in the quiescent vasculature, however, it is induced dramatically at sites of endothelial cell activation and vascular remodeling. Ang2 expression is induced by various cytokines, including VEGF and fibroblast growth factor (FGF-2), and by microenvironmental factors. Ang2 is upregulated together with VEGF-A at sites of angiogenic sprouting, whereas reduced VEGF-A expression relative to Ang2 is associated with vascular regression. (Eklund L. and Olsen B,R, 2006 Exp Cell Res 312:630; Shim W.S.N, et al, 2007 Mol Cancer Res 5(7):655). Angl-mediated Tie2 signaling functions as the default pathway to control vascular quiescence. Angl exerts a protective effect on the endothelium and limits its ability to be activated by exogenous cytokines, thus controls vascular homeostasis and endothelial activation. Proper vascular homeostasis is tightly controlled by balanced Tie2 signaling. Ang2 expression is tightly controlled as well. The release of Ang2 results in rapid destabilization of the endothelium. Moreover, Ang2 triggers an inflammatory response by activating the endothelium and inducing permeability. (Fiedler U. and Augustin KG., 2006 TRENDS Immun 27(12); 5 52). Ang3 and Ang4 are not well studied but are believed to be interspecies orthologues between mouse and human, respectively (Valenzuela DM., et at, 1999 Proc Natl AcadSci USA 96:1904-9). The function of Ang3 and Ang4 in angiogenesis is controversial compared with the more established members of the family. Ang3 has been reported to act as antagonist that interfers with Angl activation of Tie2 and Akt in tumor growth. However, Ang3 was found to strongly activate mouse Tie2, but not its human counterpart, wheras Ang4 did not desplay species selectivity in Tie2 activation (Shim W.S.N., et al, 2007 Mol Cancer Res 5(7):655). Angiogenic inhibitors are being vigorously pursued. Currently, several angiogenic inhibitors including bevacizumab (Avastin), thalidomide (Thalomid), lenalidomide (Revlimid), ranibizumab (Lucentis), sutinib (Sutent), sorafenib (Nexavar), and pegaptanib (Macugen) are in clinical use. Several angiogenic inhibitors including bevasiranib, AGN-211745, TG-100801, volociximab, ATG-003, relimid, RTP-8011-14, aflibercept, apremilast, INGN-241, angiostatin, endostatin are in clinical trials and many others are in development. The anti-angiogenic compounds developed include monoclonal antibodies or antibody fragments (e.g. bevacizumab, ranibizumab, and volociximab), aptamers (e.g. pegaptanib and E-10030), small-molecules (e.g. thalidomide, ATG-003, TG-100801, pazopanib, vandetanib, lenalidomide, and cediranib), gene therapy (e.g. angistat, advexin, and HslGN-241), recombinant proteins (e.g. aflibercept, ABT-828, and replistatin), small interfering RKA (siRNA, e.g. AGN-211745 and bevasiranib), and peptides (e.g. ABT-510, angiostatin, endostatin). However, as in all technologies in all times, there is an ongoing need for new improved compounds navi'ng anti-angibgemc activity. SUMMARY OF THE INVENTION In at least some embodiments, the subject invention now provides novel peptides corresponding to segments of Angl, Ang2, and Ang4, homologs thereof, orthologs thereof, derivatives thereof, antibodies directed thereto, and fusion proteins comprising them, all of which have a therapeutic value for a wide range of conditions, disorders and diseases. According to some embodiments of the present invention the conditions, disorders and diseases are conditions, disorders and diseases where treatment or prevention of undesired angiogenesis can be of therapeutic value. Such conditions, disorders and diseases include, but are not limited to cancer, respiratory diseases, metabolic disorders, fibrotic and connective tissue related conditions, urogenital disorders, ocular diseases, vascular anomalies, cardiovascular diseases and their complications, inflammatory conditions associated with an infection, inflammatory disorders, chronic inflammatory diseases, autoimmune diseases, bone disease or bone-related disorder and pain. Other diseases associated with undesired angiogenesis will be apparent to those skilled in the art. In at least some embodiments, the subject invention thus provides a peptide consisting essentially of an amino acid sequence LKEEKENLQGLVTRQTYIIQELEKQLNRAT (CGEN-H2 [SEQ ID NO: 1]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence TNNSVLQKQQL (CGEN-H3 [SEQ ID NO: 2]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence LMDTVHNLVNL (CGEN-A8 [SEQ ID NO: 3]} or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence NEILKIHEKNSLLEHKILEMEGKHK (CGEN-H7 [SEQ ID NO: 4]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QLQVLVSKQNSUEEL (CGEN-G4 [SEQ ID NO: 5]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence DLMETVNNLLTMMSTSNSAKD (CGEN-G6 [SEQ ID NO: 6]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QEELASHSKKAKLLNTLSRQSAALTNIERGLRGVR (CGEN-F9 [SEQ ED NO: 7]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QHSLRQLLVLLRHLVQERANASA (CGEN-F12 [SEQ ED NO: 8]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence TDMEAQLLKQTSRMDAQM (CGEN-C6 [SEQ ID NO: 9]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence ETFLSTNKLENQ (CGEN-A11 [SEQ ID NO: 10]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence TQQVKQLEQALQNNTQWLKKLERAIKTIL (CGEN-G2 [SEQ ID NO: 11]) or a homolog or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-H2 peptide consisting essentially of an amino acid sequence EGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQ [SEQ ED NO: 12] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-H3 peptide consisting essentially of an amino acid sequence QELEKQLNRATTNNSVLQKQQLELMDTVHNLV [SEQ ID NO: 13] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-A8 peptide consisting essentially of an amino acid sequence NSVLQKQQLELMDTVHNLVNLCTKEGVLLKG [SEQ ID NO: 14] or a derivative thereof. In at least some embodiments, the subject invention farther provides a homolog of a CGEN-H7 peptide consisting essentially of an amino acid sequence laEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEK [SEQ ID NO: 15] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-G4 peptide consisting essentially of an amino acid sequence QLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVN [SEQ ID NO: 16] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a NNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQIS [SEQ ID NO: 17] or a derivative thereof. In at least some embodiments, the subject invention farther provides a homolog of a CGEN-F9 peptide consisting essentially of an amino acid sequence KRLQALETKQQEELASILSKKAKLLNTLSRQSAALTNIERGLRGVRHNSSLLQDQ Q [SEQ ID NO: 18] or a derivative thereof. In at least some embodiments, the subject invention farther provides a homolog of a CGEN-F12 peptide consisting essentially of an amino acid sequence RHNSSLLQDQQHSLRQLLVLLRHLVQERANASAPAFIMAGEQV [SEQ ID NO: \9] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-C6 peptide consisting essentially of an amino acid sequence NQTTAQIRKLTDMEAQLLNQTSRMDAQMPETFLSTNKL [SEQ ID NO: 20] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-A11 peptide consisting essentially of an amino acid sequence QTSRMDAQMPETFLSTNKLENQLLLQRQKLQQ [SEQ ID NO: 21] or a derivative thereof. In at least some embodiments, the subject invention further provides a homolog of a CGEN-G2 peptide consisting essentially of an amino acid sequence ANPLHLGKLPTQQVKQLEQALQNNTQWLKKLERAIKTILRSKLEQVQQQ [SEQ ID NO: 22] or a derivative thereof. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence corresponding to a homolog of a peptide according to at least some embodiments of the present invention, consisting essentially of an amino acid sequence as set forth in any one of SEQ ID NOs: 63-186. In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide of at least some embodiments of the present invention. In at least some embodiments, the subject invention further provides a partner helix peptide consisting essentially of an amino acid sequence as set forth in any one of SEQ ID NOs: 48-62. In at least some embodiments, the subject invention also provides an antibody that selectively binds to an epitope in a peptide as set forth in any one of SEQ ID NOs: 1-22, 48-186. In at least some embodiments, the subject invention further provides a conjugate or fusion protein comprising a peptide as set forth in any one of SEQ ID NOs: 1-22,48-186. In at least some embodiments, the subject invention further provides a pharmaceutical composition comprising a peptide or a homolog thereof or a derivative thereof, an antibody of the invention or a fusion protein of the invention and a pharmaceutically acceptable carrier. In at least some embodiments, the subject invention further envisages a peptide of the invention or a homolog or a derivative thereof, an antibody or a fusion protein for use in therapy and further envisages a use of a peptide as described herein or a homolog or a derivative thereof, and/or an antibody or a fusion protein for the manufacture of a medicament. In at least some embodiments, the subject invention further provides a method of treating cancer comprising administering a pharmaceutically effective amount of one or more of a peptide as described herein or a homolog thereof or a derivative thereof, an antibody or a fusion protein as described herein, and a pharmaceutically acceptable carrier, to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating respiratory disease comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a metabolic disorder comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a fibrotic or connective tissue related condition comprising administering a pharmaceutical)}? effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a urogenital related disorder comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating an ocular disease comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a vascular anomaly comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a cardiovascular disease comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating an inflammatory condition associated with an infection or an inflammatory disorder comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a chronic inflammatory or autoimmune disease comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating a bone disease or bone-related disorder comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating and managing pain comprising administering a pharmaceutically effective amount of a peptide according to at least some embodiments of the present invention or a homolog thereof or a derivative thereof, an antibody according to at least some embodiments of the present invention, or a fusion protein according to at least some embodiments of the present invention and a pharmaceutically acceptable carrier to a subject in need thereof. In at least some embodiments, the subject invention also provides nucleotide sequences encoding a peptide according to at least some embodiments of the present invention or a homolog thereof. All amino acid sequences and/or nucleic acid sequences shown herein as embodiments of the present invention relate to their isolated form. The terms "polypeptide," "peptide" and "protein" are used interchangeably herein to refer to a polymer of amino acid residues. The terms encompass any peptide (including cyclic peptides) or protein comprising two or more amino acids joined to each other by peptide bonds or modified peptide bonds. "Polypeptide" refers to both short chains, commonly referred to as peptides, oligopeptides or oligomers, and to longer chains, generally referred to as proteins. "Polypeptides" include amino acid sequences modified either by natural processes, or by chemical modification techniques which are well known in the art. Modifications may occur anywhere in a polypeptide, including the peptide backbone, the amino acid side-chains, and the amino or carboxyl termini. Polypeptides can be modified, e.g., by the addition of carbohydrate residues to form glycoproteins. The terms "polypeptide," "peptide" and "protein" include glycoproteins, as well as non-glycoproteins. The terms "conjugate" and "fusion protein" and any lingual derivatives thereof are interchangeably used herein. BRIEF DESCRIPTION OF THE DRAWINGS In order to understand the invention and to see how it may be carried out in practice, embodiments will now be described, by way of non-limiting example only, with reference to the accompanying drawings, in which: Figure 1 demonstrates the effect of 1 and 20 ug/mL of CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4), CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) on in vitro angiogenesis using AngioKit (TCS Cellworks, UK) compared to untreated (UT). Figure 2: shows a multiple alignment of examples of homologous sequences of peptides according to at least some embodiments of the present invention, derived from various organisms. Rectangles show the comparison blocks for peptides of the invention with amino acid residue numbering according to the human sequence. Figure 2A shows a multiple alignment comparison of the sequence of CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), corresponding to amino acid residues 215-230 and 250-270, respectively, of the human angiopoietin 2 protein sequence (SEQ ID NO: 46), and homologous sequences derived from Macaca mulatta (gi| 109085520), Equus caballus (gi| 149742724), Sus scrofa (gi|47523224), Bos Taurus (gi|157426837), Mus musculus (gi|31982508), Rattus norvegicus (gij 109503530), Canis lupus familiaris (gi| 114326363), Monodelphis domestica (gij 126303279), Gallus gallus (gi|10120280), Ornithorhynchus anatinus (gij 149412433), Pan troglodytes (gi|l 14618691). Figure 2B shows a multiple alignment comparison of the sequence of CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4) corresponding to amino acid residues 212-241, 242-252, 254-264, 182-206, respectively, in the human angiopoietin 1 protein (SEQ ID NO: 45), and homologous sequences derived from Macaca mulatta (gi(109087219), Equus caballus (gi| 149721604), Sus scrota (gi (47522748), Bos Taurus (gi|l 16003815), Mus musculus (gi|46048213), Rattus norvegicus (gi|23308739), Canis lupus familiaris (gi|54262113), Monodelphis domestica (gi|126322207), Gallus gallus (gi| 118087303), Xenopus laevis (gi| 148238152), Pan troglodytes (gi| 114621310). Figure 2C shows a multiple alignment comparison of the sequence of CGEN-F9 (SEQ ID NO: 1), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), CGEN-G2 (SEQ ID NO: 11) corresponding to amino acid residues 210-245, 255-277, 150-167, 169-180, 84-112 respectively of the angiopoietin 4 protein sequence (SEQ ID NO: 47), and homologous sequences derived from Macaca mulatta (gi)109092550), Bos Taurus (gi| 115497116), Mus musculus (gi|6753006), Rattus norvegicus (gi| 157820699), Canis lupus familiaris (gi(73992066). Figure 3 demonstrates identification of helix-helix interactions using a unique computerized method. Figures 3A demonstrates an example for a known protein (BAG-1, Protein Data Bank ED Ihxl (chain B)) that comprises two helices that interact with each other in an anti-parallel manner. Figure 3A presents the residue-residue contact map, corresponding to the two anti-parallel helices taken from BAG-1; Figure 3B demonstrates a schematic view of two helices interacting through their adjacent faces; Figure 3C shows a typical Fourier transform corresponding to the sum of columns in the 21 by 21 matrix (a submatrix of the protein's contact map) that represents the anti-parallel interaction. Figure 4 shows a map of scores based on the Fourier transform of the predicted contact map of Ang4. The residue-residue contact map for Ang4 was calculated using SVMcon (J. Cheng, P. Baldi, BMC Bioinformatics 8, 113 (2007). Figure 5 demonstrates the capability of peptides CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-C6 (SEQ ID NO: 9), and CGEN-A11 (SEQ ID NO: 10) to interfere with the binding of Angl (Figure 5A), Ang2 (Figure 5B), or Ang4 (Figure 5C) to Tie2 using the BIACORE technology. Figure 6 demonstrates the effect of 0.5 and 5 nmole of peptides CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) on in ovo angiogenesis in the avian chorioallantoic membrane (CAM) model. Figure 7 demonstrates the effect of CGEN-A11 (SEQ ID NO: 10) on in vivo angiogenesis in rat model of oxygen-induced retinopathy (OIR). Figure 7A demonstrates the effect of CGEN-A11 (SEQ ID NO: 10) on intra-retinal vascular development. Figure 7B shows the effect of CGEN-A11 (SEQ ID NO: 10) on pre-retinal neovascular growth. DETAILED DESCRIPTION OF THE INVENTION In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence LKEEKENLQGLVTRQTYIIQELEKQLNRAT (CGEN-H2 [SEQ ID NO: 1]) or a homolog or a derivative thereof. CGEN-H2 corresponds to amino acid residues 212-241 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340; SEQ ID NO: 45). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence TNNSVLQKQQL (CGEN-H3 [SEQ ID NO: 2]) or a homolog or a derivative thereof. CGEN-H3 corresponds to amino acid residues 242-252 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence LMDTVHNLVNL (CGEN-A8 [SEQ ID NO: 3]) or a homolog or a derivative thereof. CGEN-A8 corresponds to amino acid residues 254-264 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence NEILKIHEKNSLLEHKILEMEGKHK (CGEN-H7 [SEQ ID NO: 4]) or a homolog or a derivative thereof. CGEN-H7 corresponds to amino acid residues 182-206 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QLQVLVSKQNSIIEEL (CGEN-G4 [SEQ ID NO: 5]) or a homolog or a derivative thereof. CGEN-G4 corresponds to amino acid residues 215-230 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315,SEQIDNO:46). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence DLMETVNNLLTMMSTSNSAKD (CGEN-G6 [SEQ ID NO: 6]) or a homolog or a derivative thereof. CGEN-G6 corresponds to amino acid residues 250-270 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QEELASILSKKAKLLNTLSRQSAALTNIERGLRGVR (CGEN-F9 [SEQ ID NO: 7]) or a homolog or a derivative thereof. CGEN-F9 corresponds to amino acid residues 210-245 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence QHSLRQLLVLLRHLVQERANASA (CGEN-F12 [SEQ ID NO: 8]) or a homolog or a derivative thereof. CGEN-F12 corresponds to amino acid residues 255-277 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention farther provides a peptide consisting essentially of an amino acid sequence TDMEAQLLNQTSRMDAQM (CGEN-C6 [SEQ ID NO: 9]) or a homolog or a derivative thereof. CGEN-C6 corresponds to amino acid residues 150-167 of the angiopoietin 4 protein sequence (GenBank Accession number: gi[7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence ETFLSTNKLENQ (CGEN-A11 [SEQ ID NO: 10]) or a homolog or a derivative thereof. CGEN-A11 corresponds to amino acid residues 169-180 of the angiopoietin 4 protein sequence (GenBank Accession number: gi]7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides a peptide consisting essentially of an amino acid sequence TQQVKQLEQALQNNTQWLKKLERAIKTIL (CGEN-G2 [SEQ ID NO: 11]) or a homolog or a derivative thereof. CGEN-G2 corresponds to amino acid residues 84-112 of the angiopoietin 4 protein sequence (GenBank Accession number: gi]7705276, SEQ ID NO: 47). Homologs, Orthologs, Derivatives and Other Modifications or Changes Without wishing to be limited in any way, according to at least some embodiments of the present invention there is provided one or more homologs, orthologs, derivatives and other modifications or changes to peptide sequences as described herein. Some non-limiting, illustrative examples are provided below. The term "homolog" relating to a peptide according to at least some embodiments of the present invention as used herein should be understood to encompass a peptide which has substantially the same amino acid sequence and substantially the same biological activity as CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2, respectively. Thus, a homolog may differ from the CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2 peptides by the addition, deletion or substitution of one or more amino acid residues or combinations thereof, provided that the resulting peptide retains the biological activity of CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2, respectively. Persons skilled in the art can readily determine which amino acid residues may be added, deleted or substituted (including with which amino acids such substitutions may be made) using established well known procedures. Examples of homologs of CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2 are deletion homologs containing less than all the amino acid residues of CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2, substitution homologs wherein one or more amino acid residues specified are replaced by other amino acid residues (e.g. amino acid with similar properties or by D-amino acids, or by non-natural amino acids) and addition homologs wherein one or more amino acid residues are added to a terminal or medial portion of CGEN-H2, CGEN-H3, CGEN-AS, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-A11, or CGEN-G2 respectively, all of which share the biological activity of CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-AI I, or CGEN-G2, respectiveiy. A substituted or inserted amino acid residue may or may not be encoded by the genetic code. A homolog of a polypeptide may be naturally occurring such as an allelic homolog, or may be a homolog that is not known to occur naturally. Non-naturally occurring homologs of polypeptides may be prepared by mutagenesis techniques or by direct synthesis. Generally, the homolog differs from the reference polypeptide by conservative amino acid substitutions. A "conservative amino acid substitution" may involve a substitution of a native amino acid residue with a nonnative residue such that there is little or no effect on the polarity or charge of the amino acid residue at that position. Desired amino acid substitutions (whether conservative or non-conservative) can be determined by those skilled in the art. For example, amino acid substitutions can be used to identify important residues of the peptide sequence, or to increase or decrease the affinity of the peptide. Naturally occurring residues may be divided into classes based on common side chain properties: An "acidic residue" refers to amino acid residues in D- or L-form having sidechains comprising acidic groups; "amide residue" refers to amino acids in D- or Inform having sidechains comprising amide derivatives of acidic groups; "aromatic residue" refers to amino acid residues in D- or L-form having sidechains comprising aromatic groups; "basic residue" refers to amino acid residues in D- or L-form having sidechains comprising basic groups; "hydrophilic residue" refers to amino acid residues in D- or L-form having sidechains comprising polar groups; "nonfunctional residue" refers to amino acid residues in D- or L-form having sidechains that lack acidic, basic, or aromatic groups; "neutral polar residue" refers to amino acid residues in D- or L-form having sidechains that lack basic, acidic, or polar groups; "polar hydrophobic residue" refers to amino acid residues in D- or L-form having sidechains comprising polar groups; "hydrophobic residue" refers to amino acid residues in D- or L-form having sidechains that lack basic or acidic groups. Conservative amino acid substitutions may involve exchange of a member of one of these classes with another member of the same class. Conservative amino acid substitutions may encompass non-naturally occurring amino acid residues, which are typically incorporated by chemical peptide synthesis rather than by synthesis in biological systems. These include peptidomimetics and other reversed or inverted forms of amino acid moieties. Non-conservative substitutions may involve the exchange of a member of one of these classes for a member from another class. In making such changes, according to certain embodiments, the hydropathic index of amino acids may be considered. Each amino acid has been assigned a hydropathic index on the basis of its hydrophobicity and charge characteristics. It is known that certain amino acids may be substituted for other amino acids having a similar hydropathic index or score and still retain substantially the same biological activity. In making changes based upon the hydropathic index, in certain embodiments, the substitution of amino acids whose hydropathic indices are within ±2 is included. In certain embodiments, those that are within ± 1 are included, and in certain embodiments, those within ±0.5 are included. It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity, particularly where the biologically functional protein or peptide thereby created is intended for use in immunological embodiments. In certain embodiments, the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with its immunogenicity and antigenicity, i.e., with a biological property of the protein. In making changes based upon similar hydrophilicity values, the substitution of amino acids whose hydrophilicity values are within ±2 is included, in certain embodiments, those that are within ± 1 are included, and in certain embodiments, those within ±0.5 are included. One may also identify epitopes from primary amino acid sequences on the basis of hydrophilicity. These regions are also referred to as "epitopic core regions." Examples of conservative substitutions include the substitution of one non-polar (hydrophobic) amino acid residue such as isoleucine, valine, leucine norleucine, alanine, or methionine for another, the substitution of one polar (hydrophilic) amino acid residue for another such as between arginine and lysine, between glutamine and asparagine, between glycine and serine, the substitution of one basic amino acid residue such as lysine, arginine or histidine for another, or the substitution of one acidic residue, such as aspartic acid or glutamic acid for another. The phrase "conservative amino acid substitution" also includes the use of a chemically derivatized residue in place of a non-derivatized residue, provided that such polypeptide displays substantially the same biological activity. In other examples, a peptide homoJog sequence, modified from the original peptide amino acid sequence includes at least one amino acid residue inserted or substituted therein, relative to the amino acid sequence of the original peptide sequence of interest, in which the inserted or substituted amino acid residue has a side chain comprising a nucleophilic or electrophilic reactive functional group by which the peptide is conjugated to a linker or half-life extending moiety. Examples of such a nucleophilic or electrophilic reactive functional group include, but are not limited to, a thiol, a primary amine, a seleno, a hydrazide, an aldehyde, a carboxylic acid, a ketone, an aminooxy, a masked (protected) aldehyde, or a masked (protected) keto functional group. Examples of amino acid residues having a side chain comprising a nucleophilic reactive functional group include, but are not limited to, a lysine residue, a diaminopropionic acid residue, a diaminobutytic acid residue, an ornithine residue, a cysteine, a homocysteine, a glutamic acid residue, an aspartic acid residue, or a selenocysteine residue. For example, the original peptide amino acid sequence (or "primary sequence") can be modified at one, two, three, four, five or more amino acid residue positions, by having a residue substituted therein different from the primary sequence or omitted. In certain embodiments of the present invention, amino acid substitutions encompass, non-canonical amino acid residues, which include naturally rare (in peptides or proteins) amino acid residues or unnatural amino acid residues (See, e.g., Link et at, Non-canonical amino acids in protein engineering, Current Opinion in Biotechnology, 14(6):603-609 (2003)). The term "non-canonical amino acid residue" refers to amino acid residues in D- or L-form that are not among the 20 canonical amino acids generally incorporated into naturally occurring proteins, for example, homoamino acids, cyclic amino acids and amino acids with derivatized side chains. Examples include (in the Inform or D-form; abbreviated as in parentheses): citrulline (Cit), homocitrulline (hCit), -methylcitrulline (NMeCit),-methylhomocitrulline (-MeHoCit), ornithine (Orn), -Methylornithine (-MeOrn or NMeOrn), sarcosine (Sar), homolysine (hLys or hK), homoarginine (hArg or hR), homoglutamine (hQ), -methylarginine (NMeR),-methylleucine (-MeL or NMeL), N-methylhomolysine (NMeHoK), -methylglutamine (NMeQ), norleucine (NIe), norvaline (Nva), 1,2,3,4-tetrahydroIsoquinoline (Tic), Octahydroindole-2-carboxylic acid (Oic), 3-{l-naphthyl)alanine (1-NaI), 3-(2-naphthyl)alanine (2-NaI), 1,2,3,4-tetrahydroisoquinoline (Tic), 2-indanylglycine (Igl), para-iodophenylalanine (pl-Phe), para-aminophenylalanine (4AmP or 4-Amino-Phe), 4-guanidino phenylalanine (Gui), 5 glycyllysine (abbreviated herein "K(-glycyl)" or "K(glycyl)" or "K(gly)"), nitrophenylalanine (nitrophe), aminophenylalanine (aminophe or Amino-Phe), benzylphenylalanine (benzylphe),-carboxyglutamic acid (-carboxyglu), hydroxyproline (hydroxypro), p-carboxyl-phenylalanine (Cpa),;-aminoadipic acid (Aad), -methyl valine (NMeVal),;-methyl leucine (NMeLeu),;-methylnorleucine (NMeNIe), cyclopentylglycine (Cpg), cyclohexylglycine (Chg), acetylarginine 0 (acetylarg),;-diaminopropionoic acid (Dpr),;-diaminobutyric acid (Dab), diaminopropionic acid pap), cyclohexylalanine (Cha), 4-methyl-phenyIalanine (MePhe),;-diphenyI-aIanine (BiPhA), aminobutyric acid (Abu), 4-phenyl-phenylalanme (or biphenylalanine; 4Bip),;-amino-isobutyric acid (Aib), beta-alanine, beta-aminopropionic acid, piperidinic acid, aminocaprioic acid, aminoheptanoic acid, aminopimelic acid, desmosine, diaminopimelic acid, N-ethylglycine, N-ethylaspargine, hydroxyzine, allo-hydroxylysine, isodesmosine, allo-isoleucine, N-methylglycine, N-methylisoleucine, N-methylvaline, 4-hydroxyproIine (Hyp), -carboxyglutamate,;-N,N,N-trimethyIlysine,;-N-acetyllysine, O-phosphoserme, N-acetylserine, N-formylmethionine, 3-methylhistidine, 5-hydroxylysine, -methylarginine, 4-Amino-O-Phthalic Acid (4APA), and other similar amino acids, and derivatized forms of any of these. . Among useful peptide homolog sequences (but without wishing to be limited in any way) are homolog sequences that introduce amino acid residues that can form an intramolecular covalent bridge (e.g., a disulfide bridge) or non-covalent interactions (e.g. hydrophobic, ionic, stacking) which may enhance the stability of the structure of the unconjugated or conjugated (e.g., PEGylated) peptide homolog molecule. In one embodiment, a homolog of a CGEN-H2 peptide according to at least some embodiments of the present invention is EGKHBOEELDTLKEEKENLQGLVTRQTYnQELEKQLNRATTNNSVLQKQQ [SEQ ID NO: 12] which corresponds to amino acid residues 202-251 of angiopoietm 1 protein sequence (GenBank Accession number: gi|20532340) or a derivative thereof. In another embodiment, a homolog of a CGEN-H3 peptide according to at least some embodiments of the present invention is QELEKQLNRATTNNSVLQKQQLELMDTVHNLV [SEQ ID NO: 13] which corresponds to amino acid residues 231-262 of angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340) or a derivative thereof. In another embodiment, a homolog of a CGEN-A8 peptide according to at least some embodiments of the present invention is NSVLQKQQLELMDTVHNLVNLCTKEGVLLKG [SEQ ID NO: 14] which corresponds to amino acid residues 244-274 of angiopoietin 1 protein sequence (GenBank Accession number: gi]20532340) or a derivative thereof. In another embodiment, a homolog of a CGEN-H7 peptide according to at least some embodiments of the present invention is KLEKQLLQQT^ILKIHEKNSLLEHKILEMEGKHKEELDTLKEEK [SEQ ID NO: 15] which corresponds to amino acid residues 172-216 of angiopoietin 1 protein sequence (GenBank Accession number: giJ20532340) or a derivative thereof. In another embodiment, a homolog of a CGEN-G4 peptide according to at least some embodiments of the present invention is QLQSIKEEKDQLQVLVSKQNSUEELEKKIVTATVN [SEQ ID NO: 16] which corresponds to amino acid residues 205-240 of angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315) Or a derivative thereof. In another embodiment, a homolog of a CGEN-G6 peptide according to at least some embodiments of the present invention is NNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQIS [SEQ ID NO: 17] 17 FEB 2011 which corresponds to amino acid residues 240-280 of angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315) or a derivative thereof. In another embodiment, a homolog of a CGEN-F9 peptide according to at least some embodiments of the present invention is KRLQALETKQQEELASILSKXAKLLNTLSRQSAALTNIERGLRGVRHNSSLLQDQ Q [SEQ ID NO: 18] which corresponds to amino acid residues 200-255 of angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276) or a derivative thereof. In another embodiment, a homolog of a CGEN-F12 peptide according to at least some embodiments of the present invention is RHNSSLLQDQQHSLRQLLVLLRHLVQERANASAPAFIMAGEQV [SEQ ID NO: 19] which corresponds to amino acid residues 245-287 of angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276) or a derivative thereof. In another embodiment, a homolog of a CGEN-C6 peptide according to at least some embodiments of the present invention is NQTTAQIRKXTDMEAQLLNQTSRMDAQMPETFLSTNKL [SEQ ID NO: 20] which corresponds to amino acid residues 140-177 of angiopoietin 4 protein sequence (GenBank Accession number: gi| 7705276) or a derivative thereof. In another embodiment, a homolog of a CGEN-A11 peptide according to at least some embodiments of the present invention is QTSRMDAQMPETFLSTiSfKLENQLLLQRQKLQQ [SEQ ID NO: 21] which corresponds to amino acid residues 159-170 of angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276) or a derivative thereof. In another embodiment, a homolog of a CGEN-G2 peptide according to at least some embodiments of the present invention is ANPLHLGKLPTQQVKQLEQALQNNTQWLKKLERAIKTILRSKLEQVQQQ [SEQ ID NO: 22] which corresponds to amino acid residues 74-122 of angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276) or a derivative thereof. The term "homolog" relating to a peptide according to at least some embodiments of the present invention as used herein should also be understood to encompass an ortholog. The term "ortholog" should be understood to encompass a peptide derived from a non-human origin which has substantially the same amino acid sequence and substantially the same biological activity as CGEN-H2, CGEN-H3, CGEN-A8, CGEN-H7, CGEN-G4, CGEN-G6, CGEN-F9, CGEN-F12, CGEN-C6, CGEN-All or CGEN-G2, respectively. In at least some embodiments, the subject invention thus provides an isolated peptide being an ortholog of CGEN-H2 [SEQ ID NO: 1], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 165-172, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN CGEN-H3 [SEQ ID NO: 2], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 161-164, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-A8 [SEQ ID NO: 3], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 137-140, or a derivative thereof. In at least some embodiments, the subject invention farther provides an isolated peptide being an ortholog of CGEN-H7 [SEQ ID NO: 4], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 149-154, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-G4 [SEQ ID NO: 5], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 73-76, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-G6 [SEQ ID NO: 6]), consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 63-72, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-F9 [SEQ ID NO: 7], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 98-102, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-F12 [SEQ ID NO: 8], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 106-110, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-C6 [SEQ ID NO: 9], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 116-118, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-A11 [SEQ ID NO: 10], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 134-136, or a derivative thereof In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of CGEN-G2 [SEQ ID NO: 11], consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 124-128, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-H2-related sequence shown in SEQ ID NO: 12, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 141-148, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-H3-related sequence shown in SEQ ID NO: 13, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 173-179, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-A8-related sequence shown in SEQ ID NO: 14, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 155-160, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-H7-related sequence shown in SEQ ID NO: 15, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 180-186, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-G4-reIated sequence shown in SEQ ID NO: 16, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 86-92, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-G6-related sequence shown in SEQ ID NO: 17, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 77-85, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-F9-related sequence shown in SEQ ED NO: 18, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 119-123, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-F12-related sequence shown in SEQ ID NO: 19, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID ~NOs: 129-133, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-C6-reIated sequence shown in SEQ ID NO: 20, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 93-97, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-A11 -related sequence shown in SEQ ID NO: 21, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 103-105, or a derivative thereof. In at least some embodiments, the subject invention further provides an isolated peptide being an ortholog of the CGEN-G2-related sequence shown in SEQ ID NO: 22, consisting essentially of an amino acid sequence as depicted in any one of SEQ ID NOs: 111 -115, or a derivative thereof. The term "partner helix (peptide)" as used herein should be understood to encompass a peptide corresponding to an alpha helix within the parent angiopoietin 1, angiopoietin 2 and/or angiopoietin 4 protein (SEQ ID NOs: 45, 46, 47, respectively), which physically interacts with a peptide according to at least some embodiments of the present invention. In at least some embodiments, the subject invention thus further provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide according to at least some embodiments of the present invention or a homolog or a derivative thereof. In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 1. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence ATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLE (SEQ ID NO:48), corresponding to a partner helix of CGEN-H2 (SEQ ID NO: 1). This peptide SEQ ID NO:48 corresponds to amino acid residues 125-160 of the angiopoietin 1 protein sequence (SEQ ID NO: 45). In at least some embodiments, the subject invention farther provides an isolated peptide consisting essentially of an amino acid sequence LTDVETQVLNQTSRLE (SEQ ID NO:49), corresponding to a partner helix of CGEN-H2 (SEQ ID NO: I). This peptide SEQ ID NO:49 corresponds to amino acid residues 145-160 of the angiopoietin 1 protein sequence (GenBank Accession number: gij20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 2. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence ATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLE (SEQ ID NO:48), corresponding to a partner helix of CGEN-H3 (SEQ ID NO: 2). This peptide SEQ ID NO:4S corresponds to amino acid residues 125-160 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence LTDVETQVLNQTSRLE (SEQ ID NO:49), corresponding to a partner helix of CGEN-H3 (SEQ ID NO: 2). This peptide SEQ ID NO;49 corresponds to amino acid residues 145-160 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 3. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence TMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSR (SEQ ID NO:50), corresponding to a partner helix of CGEN-A8 (SEQ ID NO: 3). This peptide SEQ ID NO:50 corresponds to amino acid residues 126-158 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence LTDVETQVLNQTSRLE (SEQ ID NO:49), corresponding to a partner helix of CGEN-A8 (SEQ ID NO: 3). This peptide SEQ ID NO:49 corresponds to amino acid residues 145-160 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 4. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence LTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQ (SEQ ID NO:51), corresponding to a partner helix of CGEN-H7 (SEQ ID NO: 4). This peptide SEQ ID NO:51 corresponds to amino acid residues 145-180 of the angiopoietin 1 protein sequence (GenBank Accession number: gi|20532340, SEQ ID NO: 45). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 5. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence QTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTR (SEQ ID NO:52), corresponding to a partner helix of CGEN-G4 (SEQ ID NO: 5). This peptide SEQ ID NO:52 corresponds to amino acid residues 120-155 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of . an amino acid sequence RKLTDVEAQVLNQTTRLELQLLEHSLS'mKLEKQIL (SEQ ID NO:53), corresponding to a partner helix of CGEN-G4 (SEQ ID NQ: 5). This peptide SEQ ID NO:53 corresponds to amino acid residues 140-175 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence RKLTDVEAQVLNQTTRLELQL (SEQ ID NO:54), corresponding to a partner helix of CGEN-G4 (SEQ ID NO: 5). This peptide SEQ ID NO:54 corresponds to amino acid residues 140-160 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence VEAQVLNQTITU.ELQLLEHSLSTNKLEKQILDQTSEINKXQ (SEQ ID NO:55), corresponding to a partner helix of CGEN-G4 (SEQ ID NO: 5). This peptide SEQ ID NO:55 corresponds to amino acid residues 145-185 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence TAEQTRKLTDVEAQVLNQTTRLELQL (SEQ ID NO:56), corresponding to a partner helix of CGEN-G4 (SEQ ID NO: 5). This peptide SEQ ID NO:56 corresponds to amino acid residues 135-160 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 6. In at least some embodiments, the subject invention iurther provides an isolated peptide consisting essentially of an amino acid sequence FLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVN (SEQ ID NO:57), corresponding to a partner helix of CGEN-G6 (SEQ ID NO: 6). This peptide SEQ ID NO:57 corresponds to amino acid residues 190-240 of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 7. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence QLLVLLRHLVQERANASAPAFMAGEQVFQDCAEIQRSGAS (SEQ ID NO:58), corresponding to a partner helix of CGEN-F9 (SEQ ID NO: 7). This peptide SEQ ID NO:58 corresponds to amino acid residues 260-300 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence QLLVLLRHLVQERANA (SEQ ID NO:59), corresponding to a partner helix of CGEN-F9 (SEQ ID NO: 7). This peptide SEQ ID NO:59 corresponds to amino acid residues 260-275 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 8. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence NQTAPMLELGTSLLNQTTAQIRKLTDMEAQLLNQTSRMD (SEQ ID NO:60), corresponding to a partner helix of CGEN-F12 (SEQ ID NO: 8). This peptide SEQ ID NO:60 corresponds to amino acid residues 126-164 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 9. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence QLLVLLRHLVQERANASAPAFIMAGEQVFQDCAEIQRSGASAS (SEQ ID NO:6I), corresponding to a partner helix of CGEN-C6 (SEQ ID NO: 9). This peptide SEQ ID NO:61 corresponds to amino acid residues 260-302 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence SNTLQRESLANPLHLGKLPTQQVKQLEQALQN (SEQ ID NO:62), corresponding to a partner helix of CGEN-C6 (SEQ ID NO: 9). This peptide SEQ ID NO:62 corresponds to amino acid residues 65-96 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention provides a peptide consisting essentially of an amino acid sequence corresponding to a partner helix of a peptide having an amino acid sequence as depicted in SEQ ID NO: 10. In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence QLLVLLRHLVQERANASAPAFIMAGEQVFQDCAEIQRSGASAS (SEQ ID NO:61), corresponding to a partner helix of CGEN-A11 (SEQ ID NO: 10). This peptide SEQ ID NO:61 corresponds to amino acid residues 260-302 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47). In at least some embodiments, the subject invention further provides an isolated peptide consisting essentially of an amino acid sequence SNTLQRESLANPLHLGKLPTQQVKQLEQALQN (SEQ ID NO:62), corresponding to a partner helix of CGEN-A11 (SEQ ID NO: 10). This peptide SEQ ID NO:62 corresponds to amino acid residues 65-96 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|77052765 SEQ ID NO: 47). In at least some embodiments, the subject invention further provides an antibody that selectively binds to an epitope within a peptide according to at least some embodiments of the present invention. In one embodiment, said epitope is located in a peptide according to at least some embodiments of the present invention as depicted in any one of SEQ ID NOs: 1-11. In another embodiment, said epitope is located in a peptide according to at least some embodiments of the present invention as depicted in any one of SEQ ID NOs: 12-22. In another embodiment, said epitope is located in a peptide according to at least some embodiments of the present invention, as depicted in any one of SEQ ID NOs: 63-186. In yet another embodiment, said epitope is located in a peptide according to at least some embodiments of the present invention as depicted in any one of SEQ ID NOs: 48-62. In at least some embodiments, the subject invention further provides an antibody that selectively binds to an epitope in a helix-helix structure derived from the interaction of a peptide according to at least some embodiments of the present invention with a corresponding partner helix. In at least some embodiments, the subject invention further provides a conjugate or fusion protein comprising a peptide according to at least some embodiments of the present invention as set forth in any one of SEQ ID NOs: 1-22,48-186. A peptide according to at least some embodiments of the present invention may contain amino acids other than the 20 gene-encoded amino acids. When amino acids are not designated as either D-or L-amino acids, the amino acid is either an L-amino acid or could be either a D-or L-amino acid, unless the context requires a particular isomer. The notations used herein for the polypeptide amino acid residues are those abbreviations commonly used in the art. The less common abbreviations Abu, Cpa, Nle, Pal, Tie, Dip, 4-Fpa, and Nal stand for 2-amino-butyric acid, p-chloroPhenylalanine, norleucine, 3-pyridyl-2-alanine, tert-leucine, 2,2-diphenylalanine, 4-fluoro-phenylalanine, and 3-(2-naphthyl)-alanine or 3-(l-naphthyl)-alanine, respectively. One example of a non-naturally occurring amino acid is an omega-amino acid, e.g., beta-alanine (beta-Ala), or 3 aminopropionic (3-aP). Other examples are non-naturally occurring amino acids, e.g., sarcosine (Sar), |3 -alanine ((3 -Ala), 2,3 diaminopropionic (2,3-diaP) or alpha-aminisobutyric acid (Aib); omega-acid is beta-alanine (beta-Ala), or 3 aminopropionic (3-aP); a hydrophobic non-naturally occurring amino acid, such as t-butylalanine (t BuA), t butylglycine (t BuG), N methylisoleucine (N Melle), norleucine (Nle), methylvaline (Mvl), cyclohexylalanine (Cha), phenylglycine (Phg), Nal, (32-thienylalanine (Thi), 2 naphthylalanine (2 Nal), or 1,2,3,4-tetrahydroisoquinoline-3 carboxylic acid (Tic); a basic amino acid, such as ornithine (Orn) or homoarginine (Har); and a neutral/polar non-naturally occurring amino acid is citrulline (Cit), Acetyl Lys, or methionine sulfoxide (MSO). Non-natural amino acids are known to those skilled in the art of chemical synthesis and peptide chemistry. Non-limiting examples of non-natural amino acids (each one in L- or D-configuration) are azidoalanine, azidohomoalanine, 2-amino-5-hexynoic acid, norleucine, azidonotkucine , La-aminobutyric acid, 3-(l-naphthyl)-alanm.e, 3-(2-naphthyl)-alanine, p-ethynyl-phenylalanine, m-ethynyJ-phenylalanme, p-ethynyl-phenylalanine, p-bromophenylalanine, p-idiophenylalanine, p-azidophenylalanine, 3-(6-chloroindolyi) alanin and those listed in Table 1 below. Table 1 id Non-conventional amine Code Non-conventional amino acid Code α-aminobutyric acid Abu L-N-methylalanine Nmala α-amino-α-methylbutyrate Mgabu L-N-methy!arginine Nmarg aminocyclopropane- Cpro L-N-methylasparagine Nmasn carboxylate L-N-methylaspartic acid Nmasp aminoisobutyric acid Ait> L-N-methylcysteine Nmcys aminouorbomyl- Norb L-N-methyiglutamine Nmgia carboxylate L-N-methylglutaraic acid Nmglu cyclohexylalanine Chexa L-N-tnethylhistidine Nmhis cyciopentyiaianine Cpen L-N-methylisolleucine Nmile D-alanine Dal L-N-methylleucine Nmleu D-arginhe Darg L-N-methyllysine Nmlys D-aspartic acid Dasp L-N-methylmethionine Nmmet D-cystetne Dcys L-N-methylnorleucine Nmnle D-glutatnine Dgta L-N-methylnorvaline Mmnva D-glutamic acid Dglu L-N-methylornithJne Nmom D-histidine Dhis L-N-methylpheny!alanine Nraphe D-isoleutine Dile L-^-methylproline NlllpTO D-leucine Dleu L-N-methylserine Nmser D-lysine Dlys L-N-methylthreonme Nmtbr D-methiouine Dmet L-N-m ethyltryptophan Nmtrp D-omithine Dorn L-N-methyHyrosine Nmtyr D-phenylaianine Dphe L-N-methylvaline Nmval D-proline Dpro L-N-mefhy!erhyJgfyeine Nmetg D-serine Dser L-N-methyl-t-butylglycine Hmtbug D-threonine Dthr L-norleucine Nle D-tryptophan Dtip L-norv aline Nva D-tyrosine Dtyr Ct-methyl-aminoisobutyrate Maib D-valine DvaJ GC-methyl-y-anunobutyrate Mgabu D-α-methylalanine Dmala a-methylcyclohexylalanine Mchexa D-α-methylargjuine Dmaig (X-methylcychpentylalanme Mcpen D-α-methylasparagine Dmasn Ct-methyJ-Ct-napthylalanine Manap D-α-methylaspartate Dmasp Ct- methylpenicillamine Mpen Dα-methylcysteine Dmcys N-(4-aminobutyI)glycine Nglu D-α-methyigiiitam'me Dmgln N-{2-aminoethyl)glycine Naeg D-α-methylhistidine Dmhis N-(3 -aminopropyl)gIycine Norn D-α-methy]iso]euciJie Dmile N- amino-Ct-methylbutyrate Nmaabu D-α-methyl]eucine Dmleu 0(-napthy!aIanine Anap b-ame&iyUysine Dmlys N-benzylglycine "Nphe D-α-methylmethionine Dmmet "N-(2-carbamylethyl)glycine Ngln D-α-methylornithine Dmorn N-(caibamylmethyl)gIycine Nasn D-αmethylphenylalanine Dmphe N-(2-carboxyethyl) glycine Nglu D-α-methylproline Dmpro N-(carboxymethyl)glycine Nasp D-αt-methylserine Dmser N-cycIobutylglycine Ncbut D-αt-roethylthreonine Dmthr N-cycloheptylglycine Nchep D-α-methyltiyptophan Dmtrp N-cyclohexylglycine Nchex D-α-methyltyrosine Dmty N-cyclodecylglycine Ncdec Dα-methylvaline Dmval N-cyclododecIglycine Ncdod D-α-methylalnine Dnmala N-cy clDoctylgly cine Ncoct D-α--methy!arginine Dnmarg N-cyclopropylglycine Ncpro D-αt-methylasparagine Dmnasn N-cycloundecylglycine Nciind D-α-metbylasparatate Dnmasp N-(2^-dipbenylethyl)glycine Nbhm D-α-methylcysteine Dnmcys N-(3,3-diphenylpropyl)glycine Nbhe Dα-methylleucine Dmnleu N-(3-indolylyethyl) glycine Nhtrp D-N-methyllysine Dnmlys N-methyl-y-aminobutyrate Nmgabu N-meffaylcyclohexylalanine Nmchexa D-N-methylmethionine Dnmmet D-N-methylomithine Dnmorn N-methylcyclopetitylalanine Nmcpen N-methylglyche Nala D-N'inethylphenylalanine Dnmphe N-methylaminoisobutyrate Nmaib D-N-methylprolme Dnmpro N-{1 -methylpropyl)glycine Nile D-N-methylserine Dnmser N-{2-mefliylpropyI)glycine Nile D-N-methylserine Dnmser ■N-(2-niethylpropyl)glycine Nleu D-N-methylthreonine Dnmthr D-N-methyltiyptophan Dnmfrp N-(l-methyIethyl)gIycine Nva D-N-methyltyrosine Dnmtyr N-methyia-napthylalanine Nraanap D-N-methyWaline Dnnwal N-methylpetiicillamine Nmpen y-aminobutyric acid Gabu N-(p-hydroxyphenyl)glydne Mifyr L-/-butyiglycine Tbug N-(thiomethyI)glycine Ncys L-efhy]glycine Etg penicillamine Pen L-homophenylalanine Hphe L-a-methylalanine Mala L-α-roetftyiarginine I Marg L-a-metbylaspara^ine Masn L-α-methylaspartate Masp L-a-methyH-butylglycine Mtbug L-α-methykysteine Mcys L-methylethyiglycine Metg Lα-methylgiutamine Mgln L-a-methylgiutamate Mglu L-α-methylhistidine Mhis L-(X-methylhomo phenylalanine Mhphe L-α-methylisoleucine Mile N-(2-methyIthioe(hyi)gfycine Nmet D-N-methyfglutamine DnmgJn N<3-guanid]'nopropyI)giycine Narg D-N-methylglutamate Dnmglu N-(l-hydroxyethyl)glycine Nthr D-N-methylhistidine Dnmhis N-(hydroxyethyI)glycine Nser D-N-methylisoleucbe Dnmile ■N-(imidazolylethyl)glycine Nhis D-N-methylleucine DnmFeu N-<3-indolyIyethyI)gIycine Nhtrp D-N-methyllysine Dmnlys N-methyl-y-aminobutyrate Nmgabu N-methylcyclohexylalanine Nmchexa D-N-methylmethionine Dnmmet D-N-methylornithine Dnmom N-methylcyclopentylalanine Nmcpen K-methylglycine Nala D-N-methylphenylalanine Dnmphe N-methylamirioisobutyrate Nmaib D-N-methylproline Dnmpro N-(l-meihylpropyl)glycine Nile D-N-methylserine Dnmser ftr-(2-methylpropy])gJycine Nku D-N-metbylthreonine Dnmthr D-N-methyltryptophan Dnmtrp N-(l-methylethyl)glycine Nval D-N-methyhyrosine Dnmtyr N-methyla-nflpthylalanine Nmanap D-N-methylvaline Dnmval N-methylpenicillamine Nmpen y-aminobutyric acid Gabu N-(p-hydroxyphenyl)glycine Nhtyr L-f-butylglycine Tbug N-(1hiomethyl)glycine Ncys L-ethylglycine Etg penicillamine Pen L-homophenylalanine Hphe L-a-methylalanine Mala L-α-methylarginine Marg L-O-methylasparagine Masn L-α-methyFaspartate Masp L-a-methyl-/-butyIgIycine Mtbug L-α-methylcysteine Mcys L-methylethylglycine Metg L-α-methylglutamine Mgln L-CC-methylgtutamate Mglu Lα-methylhistidine Mhis L-CC-methylhomophenylafanine Mhphe L-α-methylisoleucine Mile N-(2-methylthioethyl)g]ycine Nmet L-α-methylleucine Mleu L-α-methyllysine Mlys L-α-methylmethionine Mmet L-α-methylnorleucine Mnle L-α-methylnorvaline Mnva L-vvv-methylomithine Mom L-α-methylphenylalanine Mphe L-v-methylproline Mpro L-α-methylserine mser L-v-methylthreonine Mthr L-α-methylvaline Mtrp L-v-methyltytosine Mtyr L-αt-methylleurine Mval nbhm Lv-methylhomophenylalanine Nmhphe N-(N-(2,2- S; 233-238 ELLGGP - > EAEGAP; 265D - > A, preferably in combination with 434N -> A; 297N - > A (for example to block N-glycosylation); 318-322 EYKCK - > AYACA; 330-331AP - > SS; or a combination thereof (see for example M. Clark, "Chemical Immunol and Antibody Engineering", pp 1-31 for a description of these mutations and their effect). The construct for the Fc chain which features the above changes optionally comprises a combination of the hinge region with the CH2 and CH3 domains. The above mutations may optional]}1 be implemented to enhance desired properties or alternatively to block non-desired properties. For example, aglycosylation of antibodies was shown to maintain the desired binding functionality while blocking depletion of T-cells or triggering cytokine release, which may optionally be undesired functions (see M. Clark, "Chemical Immunol and Antibody Engineering", pp 1-31). Substitution of 331proline for serine may block the ability to activate complement, which may optionally be considered an undesired function (see M. Clark, "Chemical Immunol and Antibody Engineering", pp 1-31). Changing 330alanine to serine in combination with this change may also enhance the desired effect of blocking the ability to activate complement. Residues 235 and 237 were shown to be involved in antibody-dependent cell-mediated cytotoxicity (ADCC), such that changing the block of residues from 233-238 as described may also block such activity if ADCC is considered, to be an undesirable function. Residue 220 is normally a cysteine for Fc from IgGl, which is the site at which the heavy chain forms a covalent linkage with the light chain. Optionally, this residue may be changed to a serine, to avoid any type of covalent linkage (see M. Clark "Chemical Immunol and Antibody Engineering", pp 1-31). The above changes to residues 265 and 434 may optionally be implemented to reduce or block binding to the Fc receptor, which may optionally block undesired functionality of Fc related to its immune system functions (see "Binding site on Human IgGl for Fc Receptors", Shields etal. vol276,pp 6591-6604, 2001). The above changes are intended as illustrations only of optional changes and are not meant to be limiting in any way. Furthermore, the above explanation is provided for descriptive purposes only, without wishing to be bound by a single hypothesis. Thus, conjugates accotding to at least some embodiments of the present invention (which comprise a peptide according to at least some embodiments of the present invention) may comprise an antigen-recognizing immunoglobulin fragment and/or Fc chain. Such immunoglobulin fragments may comprise, for example, the Fab', F (ab') 2, Fv or Fab fragments, or other antigen-recognizing immunoglobulin ^fragments. Such immunoglobulin fragments can be prepared, for example, by proteolytic enzyme digestion, for example, by pepsin or papain digestion, reductive alkylation, or recombinant techniques. The materials and methods for preparing such immunoglobulin fragments are well-known to those skilled in the art. See Parham, J. Immunology, 131,2895, 1983; Lamoyi et al, J. Immunological Methods, 56,235,1983. In at least some embodiments, the subject invention thus provides a conjugate/ fusion protein comprising a peptide according to at least some embodiments of the present invention as depicted in any one of SEQ ID NOs: 1-22 and 48-186. In at least some embodiments, the subject invention provides a conjugate/fusion protein according to at least some embodiments of the present invention for use in therapy. In at least some embodiments, the subject invention also provides a use of a conjugate/fusion protein according to at least some embodiments of the present invention for the manufacture of a medicament. In at least some embodiments, the subject invention further provides a pharmaceutical composition comprising a conjugate or fusion protein according to at least some embodiments of the present invention. In at least some embodiments, the subject invention further provides a method of treating conditions, disorders and diseases where' treatment or prevention of undesired angiogenesis can be of therapeutic value, comprising administering a pharmaceutically effective amount of a conjugate or fusion protein according to at least some embodiments of the present invention or a pharmaceutical composition comprising such conjugate or fusion protein to a subject in need thereof. In at least some embodiments, the subject invention further provides a method of treating conditions, disorders and diseases, selected from but not limited to cancer, respiratory diseases, metabolic disorders, fibrotic and connective tissue related conditions, urogenital disorders, ocular diseases, vascular anomalies, cardiovascular diseases and their complications, inflammatory conditions associated with an infection or inflammatory disorders, chronic inflammatory and autoimmune diseases, bone disease or bone-related disorder and pain, comprising administering a pharmaceutically effective amount of a conjugate or fusion protein according to at least some embodiments of the present invention or a pharmaceutical composition comprising such conjugate or fusion protein to a subject in need thereof. The following abbreviations should be understood as follows: Amino Acid Abbreviation IUPAC Symbol: A = Ala = Alanine C = Cys = Cysteine D = Asp = Aspartic Acid E = Glu = Glutamic Acid F = Phe = PhenylAlanine G = Gly = Glycine H = His = Histidine I = lie = Isoleucine L = Lys = Lysine M = Met = Methionine N = Asn = Asparagine P = Pro = Proline Q = Gin = Glutamine R = Arg = Arginine S = Ser = Serine T = Thr = Threonine V = Val = Valine W = Trp = Tryptophan Y = Tyr = Tyrosine The following abbreviations shall be employed for nucleotide bases: A for adenine; G for guanine; T for thymine; U for uracil; and C for cytosine. The invention is iurther described in the following examples, which are not in any way intended to limit the scope of the present invention as claimed. EXAMPLES EXAMPLE 1 - Synthesis of peptides according to at least some embodiments of the present invention The peptides were synthesized by solid-phase peptide synthesis using Fmoc-chemistry at Pepscan Systems (http://www.pepscan.nl). The peptides were amidated at their C-terminus, and acetylated at their N-terminus. CGEN-H2 (SEQ ID NO: 1) has a molecular weight of 3628.3, CGEN-H3 (SEQ ID NO: 2) has a molecular weight of 1313.6, CGEN-A8 (SEQ ID NO: 3) has a molecular weight of 1268.4, CGEN-H7 (SEQ ID NO: 4) has a molecular weight of 3052.7, CGEN-G4 (SEQ ID NO: 5) has a molecular weight of 1882.3, CGEN-G6 (SEQ ID NO: 6) has a molecular weight of 2356.8, CGEN-F9 (SEQ ID NO: 7) has a molecular weight of 4006.8, CGEN-F12 (SEQ ID NO: 8) has a molecular weight of 2694.3, CGEN-C6 (SEQ ID NO: 9) has a molecular weight of 2124.5, CGEN-A11 (SEQ ID Nular weight of 3506.2 1. CGEN-H2 [SEQ ID NO: 1]O: 10) has a molecular weight of 1464.7, and CGEN-G2 (SEQ ID NO: 11) has a molec LKEEKENLQGLVTRQTYlIQELEKQLNRAT 2. CGEN-H3 [SEQ ID NO: 2] TNNSVLQKQQL 3. CGEN-A8 [SEQ ID NO: 3] LMDTVHNLVNL 4. CGEN-H7 [SEQ ID NO: 4] NEILKIHEKNSLLEHKILEMEGKHK 5. CGEN-G4 [SEQ ID NO: 5] QLQVLVSKQNSIIEEL 6. CGEN-G6 [SEQ ID NO: 6] DLMETVNNLLTMMSTSNSAKD 7. CGEN-F9 [SEQ ID NO: 7] QEELASILSKKAKLLNTLSRQSAALTNIERGLRGVR 8. CGEN-F12 [SEQ ID NO: 8] QHSLRQLLVLLRHLVQERANASA 9. CGEN-C6 [SEQ ID NO: 9] TDMEAQLLNQTSRMDAQM 10. CGEN-A11 [SEQ ID NO: 10] ETFLSTNKLENQ 11. CGEN-G2 [SEQ ID NO: 11] TQQVKQLEQALQNNTQWLKKLERAIKTIL EXAMPLE 2 - Analysis of activity of peptides according to at least some embodiments of the present invention on angiogenesis in vitro CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), . CGEN-H7 (SEQ ID NO: 4), CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) as synthesized in Example 1, were analyzed for their ability to affect angiogenesis in vitro in a human multicellular model (AngioKit, TCS CellWorks, UK). This model reproduces the different phases of the angiogenesis process using a co-culture of human endothelial cells with other human cell types in specially developed medium (Bishop E.T. et al, 1999 Angiogenesis 3(4):335). Briefly, 24 well plates were seeded with cells on day 0 and medium was changed on days 3, 4, 7, 10 and 12 in accordance with the standard AngioKit procedure. Test and control compounds at the appropriate dilutions were included in the medium changes on days 4,7, 10 and 12. CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) were dissolved in 20% DMSO and CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), and CGEN-C6 (SEQ ID NO: 9) were dissolved in 1% NH4HCO3 to a stock concentration of lmg/ml. All test samples were diluted in medium to their final concentration on the day that they were added to the appropriate wells. Peptides were assayed at two concentrations (1 and 20ug/mL) in duplicates. The following control treatments were included: "untreated" optimized growth medium, suramin (20uM) as anti-angiogenic control, Tie-2 neutralizing antibody (R&D Systems, Cat# AF313, 5ug/ml) as anti-angiogenic inhibitor of the Ang/Tie2 pathway, VEGF (2ng/mL) as pro-angiogenic control, and treatments of the appropriate buffers; DMSO or NH4HCO3, as vehicle controls. All AngioKits were then fixed and stained on day 14, using the CD31 Staining Kits according to the standard AngioKit procedure. Comparison of tubule development was conducted using the "AngioSys" (TCS Cellworks, UK) image analysis system developed specifically for the analysis of images produced using the AngioKit. Four images taken from predetermined positions within each well were recorded. Each concentration of test compound therefore yielded 4 images for analysis in duplicate. Figure 1 demonstrates the effect of CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4), CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ED NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) on in vitro angiogenesis. CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4), CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) were added at 1 or 20 ug/mL to a commercial co-culture (Angiokit) of early passage human endothelial cells with early passage human interstitial cells and the total tubule length was measured after 14 days. The results, shown in Figure 1, are given as total tubule length relative to the untreated growth medium, defined as 100%. As shown in Figure 1, CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4), CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ED NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) reduced total tubule length by 15-36%. VEGF induced tubule length by 130%, wheras the Tie-2 neutralizing antibody control and the positive anti-angiogenic control, suramin, reduced the tubule length by 32% and 50%, respectively (data not shown). EXAMPLE 3: Ortholoes The sequence of the CGEN-H2 (SEQ ©NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID NO: 4) corresponding to amino acid residues 212-241,242-252,254-264,182-206, respectively, in the human angiopoietin 1 protein (SEQ ID NO: 45) is highly conserved throughout other species and orthologs, as can be seen from Figure 2B. Figure 2B shows a multiple aiignment comparison of the sequence of CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), CGEN-H7 (SEQ ID "NO: 4) corresponding to amino acid residues 212-241, 242-252, 254-264, 182-206, respectively, in the human angiopoietin 1 protein (SEQ ID NO: 45), and homologous sequences derived from various organisms, including Macaca mulatta (gi| 109087219), Equus caballus (gij 149721604), Sus scrofa (gi|47522748), Bos Taurus (gi|l 16003815), Mus muscuhis (gi|46048213), Rattus norvegicus (gi|23308739), Cams lupus familiaris (gi|54262113), Monodelphis domestica (gi| 126322207), Gallus gallus (gi| 118087303), Xenopus laevis (gi| 148238152), Pan troglodytes (gi|l 14621310). The rectangles show the comparison blocks for the peptides. Positions of the peptides are identified according to human angiopoietin 1 protein (SEQ ID NO: 45). The sequences of orthologous peptides for CGEN-H2 (SEQ ID NO: 1), CGEN-H3 (SEQ ID NO: 2), CGEN-A8 (SEQ ID NO: 3), and CGEN-H7 (SEQ ID NO: 4) are provided in SEQ ID NO: 165-172,161-164,137-140, and 149-154, respectively. The sequence of the CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), corresponding to amino acid residues 215-230 and 250-270, respectively, of the angiopoietin 2 protein sequence (GenBank Accession number: gi|4557315, SEQ ID NO: 46) is highly conserved throughout other species and orthologs, as can be seen from Figure 2A. Figure 2A shows a multiple alignment comparison of the sequence of CGEN-G4 (SEQ ID NO: 5), CGEN-G6 (SEQ ID NO: 6), corresponding to amino acid residues 215-230 and 250-270, respectively, of the human angiopoietin 2 protein sequence (SEQ ID NO: 46), and homologous sequences derived from various organisms, including Macaca mulatta (gi| 109085520), Equus caballus (gi| 149742724), Sus serofa (gi|47523224), Bos Taurus (gi|l57426837), Mus musculus (gi|31982508), Rattus norvegicus (gi| 109503530), Canis lupus familiaris (gi| 114326363), Monodelphis domestica (gi| 126303279), Gallus gallus (gij 10120280), Ornithorhynchus anatinus (gijl49412433), Pan troglodytes (gi|l 14618691). The rectangles show the comparison blocks for the peptides. Positions of the peptides are identified according to human angiopoietin 2 protein (SEQ ID NO: 46). The sequences of orthologous peptides for CGEN-G4 (SEQ ID NO: 5), and CGEN-G6 (SEQ ID NO: 6) are provided in SEQ ID NO: 73-76, and 63-72, respectively. The sequence of the CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-AI1 (SEQ ID NO: 10), CGEN-G2 (SEQ ID NO: 11) corresponding to amino acid residues 210-245,255-277,150-167,169-180, 84-112 of the angiopoietin 4 protein sequence (GenBank Accession number: gi|7705276, SEQ ID NO: 47) is highly conserved throughout other species and orthologs, as can be seen from Figure 2C. Figure 2C shows a multiple alignment comparison of the sequence of CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), CGEN-G2 (SEQ ID NO: 11) corresponding to amino acid residues 210-245, 255-277, 150-167, 169-180, 84-112 of the angiopoietin 4 protein sequence (GenBank Accession number: gi [7705276, SEQ ID NO: 47), and homologous sequences derived from various organisms, including Macaca mulatta (gi| 109092550), Bos Taurus (gi]l 15497116), Mus musculus (gi|6753006), Rattus norvegicus (gi| 157820699), Canis lupus familiaris (gi[73992066). The rectangles show the comparison blocks for the peptides. Positions of the peptides are identified according to human angiopoietin 4 protein (SEQ ID NO: 47). The sequences of orthologous peptides for CGEN-F9 (SEQ ID NO: 7), CGEN-F12 (SEQ ID NO: 8), CGEN-C6 (SEQ ID NO: 9), CGEN-A11 (SEQ ID NO: 10), and CGEN-G2 (SEQ ID NO: 11) are provided in SEQ ID NO: 98-102, 106-110, 116-119, 134-136, and 124-128, respectively. EXAMPLE 4 design of conformational change blockers of Angiopoietins Conformational changes in proteins play a major role in activity regulation. Natural and synthetic molecules that modulate such changes are of considerable biological importance. Such molecules include allosteric effectors that alter the rapidity of enzyme-catalyzed reactions (J. Monod, et ah, J Mol Biol 12, 88 (1965)), molecules that shift the oligomerization equilibrium of proteins (Z Hayouka et ah, Proc Natl Acad Sci USA 104, 8316 (2007)), and molecules that interfere with transmembrane helix-helix associations (H. Yin et ah, Science SI5,1817 (2007)). Conformational change modulators of Angiopoietins were designed. The designed peptides were identified using a unique computerized method to interfere with conformational changes involving helix-helix interactions. A computational approach for sequence-based identification of infra-molecular helix-helix interactions was able to detect interactions that ordinarily difficult to observe experimentally. The computational approach was based on the analysis of correlated mutations in the sequences of a target protein and its homologs (Figure 3and Figure 4). Such analysis aims at identifying intra-molecular interactions between pairs of amino acid residues (S. S. Choi, et ah, Nat Genet 37, 1367 (2005); G. B. Gloor, et ah, Biochemistry 44, 7156 (2005); U. Gobel, et ah, Proteins 18, 309 (1994); S. W. Lockless, et ah, Science 286, 295 (1999); L. C. Martin, et ah, Bioinformatics 21, 4116 (2005); F. Pazos, et al., Comput Appl Biosci 13, 319 (1997)) facilitated by the introduction of a new category of residue-residue contact prediction into the Critical Assessment of techniques for protein Structure Prediction (CASP) competition (J. M. Izai-zugaza, etah, Proteins 69 Suppl 8, 152 (2007)). Nevertheless, despite these algorithmic advances and the growing availability of sequence data, the signal to noise ratio of correlated mutation analysis remains relatively low, and does not currently allow ab initio structure prediction. The detection of interacting segments through correlated mutation analysis is hindered by the thus low signal to noise ratio, when applied naively, e.g., averaging over a sliding window approach. The conceptual new ingredient of the unique in silico approach used herein for identification of peptides capable of acting as conformational change blockers of Angiopoietins, was the exploitation of the periodic nature of the correlated mutation data for helix-helix interactions, for which the corresponding periodicity should be around 3.6 amino acids (Figures 3A-B). Technically, this was achieved using an appropriate application of the Fourier transform. An interaction in Ang4 was detected by a peak in the absolute value of the Fourier transform of the correlated mutations signal around the typical periodicity (Figure 3C). Although the transform is one dimensional, it analyses the two dimensional matrix of correlated mutation scores, detecting the periodicity manifested in both interacting segments (Figures 4). In this unique technology, used for computerized detection of peptides capable of acting as conformational change blockers of Angiopoietins, Fourier transform was introduced to correlated mutations analysis, substantially improving the signal to noise ratio, as well as a "two dimensional" Fourier analysis was employed in protein structure determination. This newly-developed tool was applied to Angl, Ang2, and Ang4, and resulted in detection of remarkable peaks of the absolute values of the Fourier transform around the expected periodicity. Using this approach, an interaction between CGEN-F9 (SEQ ID NO:7) and a helix peptide corresponding to SEQ ID NO.58-59 in Aug 4 (partner helix) was computationally identified. Figure 3 shows the identification using the unique computerized method for prediction of helix-helix interactions. Figure 3A demonstrates an example of residue-residue contact map of two anti-parallel helices taken from the solved structure of BAG-1 (PDB id: 1HX1 Chain B) calculated using CSU (V. Sobolev, A. Sorokim, J. Prilusky, K E. Aboia, M. Edelman, Bioinformatics 15, 327 (1999)). Figure 3B demonstrates a schematic view of two helices interacting through their adjacent faces. This interaction gives rise to the 3.6-residue periodicity that is the basis of our Fourier transform-based approach. Each residue on one helix may interact with 3-4 residues on the other helix spanning a region of 8-9 residues (see rectangle in Figure 3A). The residue-residue contact map for Ang 4 was predicted by SVMcon (J. Cheng, et al, BMC Bioinformatics 8, 113 (2007)). Typically, in these methods {S. S. Choi, Nat Genet 37, 1367 (2005); G. B. Gbor, Biochemistry 44, 7156 (2005); U. Gobel, et al, Proteins 18, 309 (1994); I. C. Martin, et al, Bioinformatics 21, 4116 (2005); F. Pazos, et al, Comput Appl Biosci 13, 319 (1997); J. Cheng, etal, BMC Bioinformatics 8, 113 (2007); S. D. Dimn, etal, Bioinformatics 24, 333 (2008); G. Shackelford, et al, Proteins 69 Suppl 8, 159 (2007)) the sequences of the protein of interest and its homologs are used for constructing a multiple sequence alignment (MSA). Correlations between columns in the MSA (correlated mutations) point to predicted residue-residue interactions. Until today however, known contact map prediction technologies suffered from low recall and low precision. These drawbacks in helix-helix interactions identification have now been solved by the unique in silico approach used herein for identification of peptides capable of acting as conformational change blockers of Angiopoietins. Figure 4 shows a map of scores based on the Fourier transform of the correlated mutation signal of Ang 4. In order to detect helix-helix interactions, for each pair of 21-residue long segments two vectors of sums of the predicted residue-residue scores were calculated: one for the rows and one for the columns of the corresponding 21 by 21 matrix. For the detection of parallel helix-helix interactions only the principal (i.e. major) diagonal and its 4 neighboring diagonals from each side were summed. For anti-parallel interactions, the minor diagonal was similarly utilized. The two vectors are then Fourier transformed. A joint score was calculated that is non-zero only if a significant peak representing a periodicity of about 3.6 residues exists in the Fourier Transform of both the 'rows' and the 'column' vectors. Figure 4 presents In Silico detection of a helix-helix interaction in Ang 4. Similar to the way the intra-molecular helix-helix that involves CGEN-F9 (SEQ ID NO:7) was detected, the computational analysis revealed other intra-molecular helix-helix interaction in Angl, Ang2, and Ang4. The results are the peptides corresponding to SEQ ID NO: 1-11 and their partner helix described as SEQ ID NO:48-62. EXAMPLE 5 - Binding analysis of peptides according to at least some embodiments of the present invention to recombinant Angl. Ang2, and Ang4 The capability of CGEN-H2 [SEQ ID NO: 1], CGEN-H3 [SEQ ID NO: 2], CGEN-A8 [SEQ ID NO: 3], CGEN-H7 [SEQ ID NO: 4], CGEN-G4 [SEQ ID NO: 5], CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] to specifically bind to recombinant Angl, Ang2, and Ang4 was investigated using the BIACORE technology, measuring protein-protein interaction and binding affinity (Wendler et al 2005, Anal Bioanal Chem, 381:1056-1064). The technology is based on surface plasmon resonance (SPR), an optical phenomenon that enables detection of unlabeled interactants fn real time. The SPR-based biosensors can be used in determination of active concentration, screening and characterization in terms of both affinity and kinetics. Peptide-protein binding was analyzed using surface plasmon resonance. Analysis of the interaction between CGEN-H2 [SEQ ID NO: 1], CGEN-H3 [SEQ ID NO: 2], CGEN-A8 [SEQ ID NO: 3], CGEN-H7 [SEQ ID NO: 4], CGEN-G4 [SEQ ID NO: 5], CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] peptides and recombinant human Angl carrier-free (R&D Systems, Cat# 923-AN-025/CF, Lot# FHW1507031), human Ang2 carrier-free (R&D Systems, Cat# 623-AN-025/CF, Lot# BNO0457121), and human Ang4 carrier-free (R&D Systems, Cat# 964-AN-025/CF, Lot# ELM025121) was conducted using the BIAcore biosensor (Pharmacia Biosensor, Uppsala, Sweden). The recombinant Angl, Ang2, and Ang4 were immobilized directly to a CM5 sensor chip. Solutions containing 10-50uM of CGEN-H2 [SEQ ID NO: 1], CGEN-H3 [SEQ ID NO: 2], CGEN-A8 [SEQ ID NO: 3], CGEN-H7 [SEQ ID NO: 4], CGEN-G4 [SEQ ID NO: 5], CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 . [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] peptides were injected into the sample chamber of the BIACORE device at a rate of 20ui/min and the interaction was monitored using surface plasmon resonance. Peptides CGEN-H2 [SEQ ID NO: 1], CGEN-H3 [SEQ ID NO: 2], CGEN-A8 [SEQ ID NO: 3], CGEN-H7 [SEQ ED NO: 4], and CGEN-G4 [SEQ ID NO: 5] showed none or low binding to the chip, possibly due to technical problems. CGEN-C6 [SEQ ID NO: 9] did not bind Angl and Ang4. Binding of CGEN-C6 to Ang2 was not sufficiently strong and too noisy for kinetic measurements or determination of affinity constant. Peptides CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGJBN-F12 [SEQ ID NO: 8], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] were capable of binding to immobilized Angl, Ang2, and Ang4 on the chip and were further analyzed for binding kinetics, as follows. Solutions containing different concentrations of CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] peptides (as indicated in Table 2) were injected into the sample chamber of the BIACORE device at a rate of 30jil/min and the interaction was monitored using surface plasmon resonance. As a background, the solutions were also injected onto an empty flow cell with no immobilized ligand and the binding levels achieved were subtracted. Data was analyzed using BIAevaluation software. The affinity constant of the interaction between CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] and Angl, Ang2, or Ang4 was determined by direct kinetic analysis. The 1:1 Langmuir binding model was used to fit kinetic data. Table 2 summarizes results of analysis of CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] interaction with Angl, Ang2, or Ang4. Kinetic measurements were done at the indicated concentration range, and they are presented as KD (M). CGEN-F12 [SEQ ID NO: 8] bound to Angl and Ang4 with high affinity. The specificity of this binding is not clear. Table 2 Peptide Cone. OiM) range Angl Ang2 Ang4 CGEN-F12 0.625-0.039 1.88xl0y 5.84xl0"b 2.43xl0"10 CGEN-G6 1.25-0.039 1.33x10"* ND 2.21xl0"8 CGEN-F9 25-1.56 2.14x10"' 3.07X10"6 2.82x10"6 CGEN-A11 25-1.56 6.74x10° 2.36xl0"6 3.69X10"6 CGEN-G2 0.625-0.039 L74xl0"8 5.66x10'" 2.5x10s EXAMPLE 6 ~ Binding analysis of peptides according to at least some embodiments of the present invention to recombinant Tie2 and competition with ligand binding to Tie-2 The capability of CGEN-G6 [SEQ ID NO: 6], CGEN-F9 {SEQ ID NO: 7], CGEN-C6 [SEQ ID NO: 9], CGEN-AI1 [SEQ ID NO: JO], and CGEN-G2 [SEQ ID NO: II] to specifically bind to recombinant Tie2 and interfere with the binding of Angl, Ang2, or Ang4 to Tie2 was investigated using the BIACORE technology, measuring protein-protein interaction arid binding affinity (Wendler et al 2005, Anal Bioanal Chem, 381: 1056-1064). The technology is based on surface plasmon resonance (SPR), an optical phenomenon that enables detection of unlabeled interactants in real time. The SPR-based biosensors can be used in determination of active concentration, screening and characterization in terms of both affinity and kinetics. Peptide-protein interaction was analyzed using surface plasmon resonance. Analysis of the interaction between CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] peptides and recombinant human Tie-2/Fc chimera (carrier-free, R&D Systems, Cat# 313-TI, Lot# BKC0707121) was conducted using the BIAcore biosensor (Pharmacia Biosensor, Uppsala, Sweden). The recombinant Tie-2/Fc chimera was immobilized directly to a CM5 sensor chip. Solutions containing 10-50uM of CGEN-G6 [SEQ ID NO: 6]t CGEN-F9 [SEQ ID NO: 7], CGEN-C6 (SEQ ID NO: 9], CGEN-AU [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] were injected into thel sample chamber of the BIACORE device at a rate of 20u.l/min and the interaction was monitored using surface plasmon resonance. In addition, solutions containing 100-500nM of Angl, Ang2, and Ang4 proteins were injected alone or in combination with 10-50u.M of CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: 11] peptides at a constant ratio of 1:100 (Ang ligand to peptide) into the sample chamber of the BIACORE device at a rate of 20ul/min and the interaction was monitored using surface plasmon resonance. CGEN-G2 [SEQ ID NO: 11] peptide showed some non specific binding and its capability to interfere with Ang ligand binding to Tie2 was not determined. Figure 5 shows the inhibition of Angl, Ang2, and Ang4 binding to Tie2 immobilized to the chip by the various peptides, as we]] as their direct binding to immobilized Tie2. Binding of Angl to Tie2 was reduced by up to 34% after incubation with CGEN-G6 [SEQ ID NO: 6], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-F9 [SEQ ID NO: 7] peptides (Figure 5A). Binding of Ang2 to Tie2 was reduced by 91-100% after incubation with CGEN-G6 [SEQ ID NO: 6] and CGEN-C6 [SEQ ID NO: 9], and to a lesser extent after incubation with CGEN-A11 [SEQ ID NO: 10] and CGEN-F9 [SEQ ID NO: 7] peptides (Figure 5B). Binding of Ang4 to Tie2 was reduced by 60-67% after incubation with CGEN-G6 [SEQ ID NO: 6] and CGEN-C6 [SEQ ID NO: 9], and to a lesser extent after incubation with CGEN-A11 [SEQ ID NO: 10] and CGBN-F9 [SEQ ID NO: 7] peptides (Figure 5C). Binding of peptides alone to Tie2 was negligible in most cases. EXAMPLE 7 - Analysis of activity of peptides according to at least some embodiments of the present invention on angiogenesis in ovo CGEN-G6 [SEQ ID NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ED NO: 9], CGEN-A11 [SEQ ED NO: 10], and CGEN-G2 [SEQ ED NO: 11], were analyzed for their ability to affect angiogenesis using the in ovo avian chorioallantoic membrane (CAM) model of angiogenesis, which is widely used as a model to examine compounds affecting angiogenesis (Richardson and Singh 2003, Curr Drug Targets Cardiovasc Haematol Disord., 3(2):155-85). Two positive controls were used: fumagillin as a general anti-angiogenic compound, and Tie2 neutralizing antibody as anti-angiogenic inhibitor of the Ang/Tie2 pathway. Leghorn fertilized eggs were incubated for 4 days at 37°C, when a window was opened on the egg's shell, exposing the CAM. Two different doses of peptides (0.5 and 5nmoI/CAM), Tie-2 neutralizing antibody (R&D Systems, Cat# AF313, 10|ig/ml; 0.4pg/CAM) or fumagillin (Tocris Bioscience, Cat # 1768; 5μg/CAM) were applied in a 40ul volume inside an area of 1 cm2 (restricted by a plastic ring) of the CAM on day 9 of embryo development. The appropriate vehicle controls were also tested. Forty-eight hours after treatment and subsequent incubation at 37°C, CAMs were fixed in situ, excised from the eggs, placed on slides and left to air-dry. Pictures were taken through a stereoscope equipped with a digital camera and the total length of the vessels was measured using image analysis software (NIH Image). For each group a total of 17-24 eggs from three different experiments were used. Data are presented as means+SEM and expressed as % of vehicle control. Statistical analysis (ANOVA followed by Dunnett's post-hoc test) was performed using Graph Pad. Figure 6 depict results obtained on vessel length with peptides CGEN-G6 [SEQ ED NO: 6], CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], CGEN-A11 [SEQ ID NO: 10], and CGEN-G2 [SEQ ID NO: II], compared to Tie2 neutralizing antibody (Ab) and the anti-angiogenic compound fiimagillin. Neutralizing Tie2 Ab blocked vessel length by 36%, while the angiogenesis inhibitor fumagillin blocked vessel length by 32%. From the peptides tested, treatment with CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-C6 [SEQ ID NO: 9], and CGEN-A11 [SEQ ID NO: 10], resulted in 20-40% inhibition, with CGEN-AU [SEQ ID NO: 10] having the greatest effect at 5 nmole. The extent of inhibition achieved by treatment with CGEN-F9 [SEQ ID NO: 7], CGEN-A11 [SEQ ID NO: 10] and CGEN-C6 [SEQ ID NO: 9] was similar to that of the positive controls. CGEN-G2 [SEQ ID NO: 11] and CGEN-G6 [SEQ ID NO: 6] did not inhibit angiogenesis in this system. A large number of clots were noted in most of the eggs treated with CGEN-G6 [SEQ ID NO: 6], thus, the results obtained with this peptide should be interpreted with caution. These results indicate clear anti-angiogenic activity for CGEN-F9 [SEQ ID NO: 7], CGEN-F12 [SEQ ID NO: 8], CGEN-A11 [SEQ ID NO: 10] and CGEN-C6 [SEQ ID NO: 9] and support the potential use of these peptides for the treatment of angiogenesis-related diseases. EXAMPLE 8 - Analysis of the effect of peptides according to at least some embodiments of the present invention on Tie2 signaling in order to determine whether peptides according to at least some embodiments of the present inventions inhibit Angl and/or Ang2-induced Tie2 signaling, human umbilical vein endothelial cells (EC) are isolated and used to perform Tie2 signaling studies. Human umbilical vein EC are isolated from at least three donors and pooled. Experiments are repeated three times with at least two different batches of donors. Cells are plated in 6 well dishes and treated with two doses of peptide alone or in combination with Angl or Ang2. Tie2 phosphorylation by Ang-1 is used as positive control. Cells are incubated with peptide for 15min, followed by treatment with 250ng/ml Ang-1 or Ang-2 for 5-lOmin. Cells are then lysed and the Tie2 receptor immunoprecipitated and blotted with a phosphotyrosine antibody to determine the phosphorylation levels of Tie2. In parallel, total cell lysates are used to determine the activation of ERK1/2 and Akt by using phospho-specific antibodies for the two kinases. Blots are scanned and bands are quantified using an image analysis software program. EXAMPLE 9 - Analysis of the effect of CGEN-AI1 [SEP ID NO: 101 on in vivo angiogenesis in a rodent model of oxygen-induced retinopathy. In order to assess the in vivo efficacy of CGEN-A11 [SEQ ID NO: 10] in a disease model of angiogenesis, a rodent model of oxygen-induced retinopathy (OIR) was used. Sprague Dawley rats were raised from birth through day P14 in a variable oxygen atmosphere consisting of 24-hour alternating cycles of 50% and 10% oxygen. Rats were predisposed to pathological retinal angiogenesis as a result of oxygen treatment. Upon removal from the oxygen exposure chamber on day P14, rats received intravitreal injections of CGEN-All [SEQ ID NO: 10] in one of two doses: 15ug/ml (low) or 75ug/ml (high), 100^g/ml recombinant rat Tie-2/Fc (R&D Systems, 3874-T2) or 100i4g/ml anti-VEGFR2 (Sigma, V1014) as positive controls, a combination of CGEN-A11 [SEQ ID NO: 10] at 30ug/ml and anti-VEGFR2 (100u.g/ml), or vehicle (PBS) at a volume of 5 ul An additional similar intravitreal administration took place 3 days later, on day P17. All pups were sacrificed on day P20. Both normal, intra-retinal vascular growth and abnormal, pre-retinal neovascular growth were assessed at six days post-exposure (P20) in ADPase-stained retinal flat-mounts, using widely published methods (e.g. Penn JS et al, 1991, Invest Ophthalmol Vis Set, 32(4):J147; Mcleod DS et at, 1987, Microvasc Res., 33:257-269) . All assessments were performed by a single, highly trained observer, who was blinded to treatment group. Areas of normal and abnormal vascular growth were measured via computer-assisted image analysis using high-resolution digital images of the stained retinal flat-mounts. The data were subjected to analysis of variance to determine statistical significance and a Dunnett's post hoc test to identify how the various treatment groups compared. Figure 7A shows the effect of CGEN-A11 [SEQ ID NO: 10] on intra-retinal, i.e. normal vascular development. Data are depicted using percent total retinal area vascularized. Sample sizes (10, 11 or 12) are indicated on each bar. Only CGEN-A11 [SEQ ID NO: 10] at the high concentration of 75|ig/ml and Tie-2/Fc showed a statistically significant increase in mtra-retiflaf normal vascular growth compared to the PBS control. These differences yielded statistical significance, both at pO.0001. Statistical significance was calculated using area (mm2) measurements. Figure 7B shows the effect of CGEN-A11 [SEQ ID NO: 10] on pre-retinal neovascular growth (i.e. pathological angiogenesis). Data are depicted as area vascularized (mm2). Sample sizes (10,11 or 12) are indicated on each bar. Intravitreal injection of CGEN-A11 [SEQ ID NO: 10] inhibited angiogenesis by 38.9% at the lower concentration (15ug/mi) and by 76.4% at the higher concentration (75jig^ml)J relative to PBS-injected eyes. Also, Tie-2/Fc showed a 61-9% inhibition of angiogenesis. The 75pg/ml CGEN-A11 [SEQ ID NO: 10] and lOOug/ml Tie-2/Fc study arms showed a statistically significant decrease in the pathologic effects of oxygen-induced retinopathy (p=0.0126 and p=0.0436, respectively.). At this concentration, CGEN-A11 [SEQ ID NO: 10] demonstrated a profound angiostatic potency, outperforming all other test compounds, including Tie-2/Fc (although the difference in the performance of these two treatments was not statistically significant; p=0.9643; student's t-test). Unexpectedly, the anti-VEGFR2 antibody, one of the two positive controls, did not exhibit any inhibition of neovascularization. Although the failure of this antibody to provide efficacy in this assay is atypical, it is not unprecedented, as commercial antibodies frequently demonstrate inconsistent performance from one lot to the next. There are a number of explanations for this, including the presence of endotoxin contamination in the antibody preparation. Accordingly, the CGEN-A11 [SEQ ID NO: 10] is believed to be solely responsible for the efficacy observed in the combined therapy arm, demonstrated in Figure 7B. The soluble Tie-2 chimera served as an appropriate and adequate positive control and significantly inhibited retinal neovascularization. The profound angiostatic potency of CGEN-A11 [SEQ ID NO: 10] further demonstrated the anti-angiogenic properties of this compound and its potential as a therapeutic compound for angiogenesis-related diseases. EXAMPLE 10 - Antibodies Reagents other than peptides are also used to inhibit the formation of the helix-helix interactions between the peptide according to at least some embodiments of the present invention (SEQ ID NOs: 1-11) and the segment corresponding to the partner helix of a peptide according to at least some embodiments of the present invention (SEQ CD NO:48-62). Antibodies that specifically bind to an epitope in the sequence corresponding to the peptide according to at least some embodiments of the present invention (SEQ ID NOs: 1-11) or in the partner helix of a peptide according to at least some embodiments of the present invention (SEQ ID NO:48-62) are highly effective to inhibit the formation of the helix-helix interactions between the two segments and thereby to act as modulators of Ang 1, Ang 2 and/or Ang4. Thus, antibodies that specifically bind to an epitope in a peptide according to at least some embodiments of the present invention (SEQ ID NOs: 1-11) or in the partner helix of a peptide according to at least some embodiments of the present invention (SEQ ID NO:48-62) or fragments thereof are used for treating wide range of conditions, disorders and diseases, selected from but not limited to cancer, respiratory diseases, metabolic disorders, fibrotic and connective tissue related conditions, urogenital disorders, ocular diseases, vascular anomalies, cardiovascular diseases and their complications, inflammatory conditions associated with an infection, inflammatory disorders, chronic inflammatory diseases, autoimmune diseases, bone disease or bone-related disorder and pain. It is appreciated that certain features of the invention, which are, for clarity, described in the context of separate embodiments, may also be provided in combination in a single embodiment. Conversely, various features of the invention, which are, for brevity, described in the context of a single embodiment, may also be provided separately or in any suitable subcombination. Although the invention has been described in conjunction with specific embodiments thereof, it is evident that many alternatives, modifications and variations will be apparent to those skilled in the art. Accordingly, it is intended to embrace all such alternatives, modifications and variations that fall within the spirit and broad scope of the appended claims. All publications, patents and patent applications mentioned in this specification are herein incorporated in their entirety by reference into the specification, to the same extent as if each individual publication, patent or patent application was specifically and individually indicated to be incorporated herein by reference. In addition, citation or identification of any reference in this application shall not be construed as an admission that such reference is available as prior art to the present invention. We claim: 1. . An isolated peptide consisting of an amino acid sequence as set forth in SEQ ID NO: 10, or a homolog or a derivative thereof which retain the biological activity of the peptide. 2. The peptide according to claim 1, wherein said peptide consists of an amino acid sequence as set forth in any one of SEQ ID NO: 21, SEQ ID NO: 134, SEQ ID NO: 135 or SEQ ID NO: 136, or a homolog or a derivative thereof which retain the biological activity of the peptide, 3. The peptide according to claim 1, wherein said peptide is chemically modified, wherein the chemical modification is selected from any one of: PEGylation, acetylation, acylation, amidation, ADP-ribosylation, glycosylation, GPI anchor formation, covalent attachment of a lipid or lipid derivative, methylation, myristyiation, prenylation, phosphorylation, ubiquitination. 4. A fusion protein comprising the peptide of claim 1. 5. The fusion protein of claim 4, wherein the peptide is fused to an Fc fragment. 6. A pharmaceutical composition comprising the peptide according to claim I, or the fusion protein according to claim 4, and a pharmaceutically acceptable carrier. 7. The pharmaceutical composition according to claim 6, wherein the pharmaceutically acceptable carrier is a controlled release vehicle, selected from the group consisting of biocompatible polymers, other polymeric matrices, capsules, microcapsules, nanocapsules, microparticles, nanoparticles, microspheres, bolus preparations, osmotic pumps, diffusion devices, liposomes, Hpospheres and transdermal delivery systems, implantable or not. 8. The peptide according to claim I, or the fusion protein according to claim 4, or the pharmaceutical composition according to claim 6, for use in the manufacture of a medicament. 9. The peptide, or the fusion protein, or the pharmaceutical composition according to claim 8, wherein the medicament is for use in the treatment of a disease or a condition selected from the group consisting of ocular disease, cancer, chronic inflammatory or autoimmune disease, vascular anomaly, cardiovascular disease, fibrotic or connective tissue related condition, comprising administering a pharmaceutically effective amount of the peptide according to claim 1, or the fusion protein according to claim 4, or the pharmaceutical composition according to claim 6, to a subject in need thereof, wherein said peptide or said fusion protein or said pharmaceutical composition is administered alone or in combination with another therapeutic agent, wherein the therapeutic agent Is selected from the group consisting of peptides, pepti-bodies, small molecules, chemotherapeutic agents such as cytotoxic and cytostatic agents, immunological modifiers such as interferons and interleukins, growth hormones or other cytokines, folic acid, vitamins, minerals, aromatase inhibitors, RNAi, Histone Deacetylase Inhibitors, proteasome inhibitors and antibodies, 10. The peptide, or the fusion protein, or the pharmaceutical composition according to claim 9, wherein said antibodies are selected from any one of bevacizumab and erbitux, and wherein the chemotherapeutic agent is at least one of cytotoxic and cytostatic agents, selected from any one of paclitaxel, cisplatin. vinorelbine, docetaxel, gemcitabine, temozolomide, irinotecan, 5FU, or carbop latin. 11. The peptide, or the fusion protein, or the pharmaceutical composition according to claim 9, wherein said peptide or said fusion protein or said pharmaceutical composition is administered by intravascular, intravenous, injection, infusion, oral, enteral, rectal, pulmonary, inhalation, nasal, topical, transdermal, buccal, sublingual, intravesical, intravitreal, intraperitoneal, vaginal, brain, intra-cerebroventricular, intra-cerebral, convection enhanced diffusion, CNS, intrathecal, perispinal, intra-spinal, parenteral, subcutaneous, intramuscular, intravenous, intradermal, transmucosal, or sublingual administration, or administration via an implant. 12. The peptide, or the fusion protein, or the pharmaceutical composition according to claim ] 1, wherein topical or transdermal administration of a said peptide or said fusion protein or said pharmaceutical composition includes ointments, pastes, creams, lotions, emulsions, gels, powders, solutions, sprays, inhalants, or patches. 13. The peptide, or the fusion protein, or the pharmaceutical composition according to claim 9, wherein: the ocular disease is selected from the group consisting of retinal angiogenesis disorder, ocular neovascularisation, retinopathies, including diabetic retinopathy and retinopathy of prematurity, age-related macular degeneration, macular oedema, trachoma, glaucoma, dry eye syndrome, neuro-ophthalmic disease, oculosystemic disease, eye infections, eye inflammation and corneal neovascularization; wherein the cancer is selected from the group consisting of breast cancer, cervical cancer, ovary cancer, endometrial cancer, melanoma, bladder cancer, lung cancer, pancreatic cancer, colon cancer, prostate cancer, hematopoietic tumors of lymphoid lineage, leukemia, acute lymphocytic leukemia, chronic lymphocytic leukemia, B-cell lymphoma, Burkitt's lymphoma, multiple myeloma. Hodgkin's lymphoma, Non-Hodgkin's lymphoma, myeloid leukemia, myelogenous leukemia, chronic myelogenous leukemia, thyroid cancer, thyroid follicular cancer, myelodysplastic syndrome (MDS), tumors of mesenchymal origin, fibrosarcoma, rhabdomyosarcomas, melanoma, uveal melanoma, teratocarcinoma, neuroblastoma, glioma, glioblastoma, benign tumor of the skin, renal cancer, anaplastic large-cell lymphoma, esophageal squamous cells carcinoma, hepatocellular carcinoma, follicular dendritic cell carcinoma, intestinal cancer, muscle-invasive cancer, seminal vesicle tumor, epidermal carcinoma, spleen cancer, bladder cancer, head and neck cancer, stomach cancer, liver cancer, bone cancer, brain cancer, cancer of the retina, small bowel cancer, salivary gland cancer, cancer of uterus, cancer of testicles, cancer of connective tissue, prostatic hypertrophy, myelodysplasia, Waldenstrom's macroglobinaemia, nasopharyngeal, neuroendocrine cancer myelodysplastic syndrome, mesothelioma, angiosarcoma, biliary cancer, Kaposi's sarcoma, carcinoid, oesophagogastric, fallopian tube cancer, peritoneal cancer, papillary serous mullerian cancer, malignant ascites,, gastrointestinal stromal tumor, and a hereditary cancer syndrome selected from Li-Fraumeni syndrome and Von Hippel-Lindau syndrome (VHL); wherein the cancer is invasive or metastatic; wherein the cancer is inflammation-induced cancer; wherein the chronic inflammatory or autoimmune disease is selected from the group consisting of multiple sclerosis, psoriasis, arthritis, rheumatoid arthritis, inflammatory bowel disease, systemic lupus erythematosus, ulcerative colitis, Crohn's disease, chronic bronchitis, asthma, allergy, pulmonary inflammation, vasculitis, transplant rejection, immune disorders associated with graft transplantation rejection, benign lymphocytic angiitis, lupus erythematosus, Hashimoto's thyroiditis, primary myxedema, Graves' disease, pernicious anemia, autoimmune atrophic gastritis, Addison's disease, insulin dependent diabetes mellitis, Good pasture's syndrome, myasthenia gravis, pemphigus, sympathetic ophthalmia, autoimmune uveitis, autoimmune hemolytic anemia, idiopathic thrombocytopenia, primary biliary cirrhosis, chronic action hepatitis, ulceratis colitis, Sjogren's syndrome, rheumatic disease, polymyositis, scleroderma, mixed connective tissue disease, inflammatory rheumatism, degenerative rheumatism, extra-articular rheumatism, collagen diseases, chronic polyarthritis, psoriasis arthropathica, ankylosing spondylitis, juvenile rheumatoid arthritis. periarthritis humeroscapularis, panarteritis nodosa, progressive systemic scleroderma, arthritis uratica, dermatomyositis, muscular rheumatism, myositis, myogelosis and chondrocalcinosis, thyroditis, allergic oedema, and granulomas; wherein the vascular anomaly is selected from the group consisting of vascular permeability, plasma leakage, venous malformation (VM), hemangioblastoma, hemangiomas, intramuscular hemangiomas, brain arteriovenous malformations (BAVM), arteriosclerosis, thrombosis, leukomalacia (PLV). Hereditary Hemorrhagic telangiectasia (HHT), Ataxia telangiectasia and Osier-Weber syndrome: wherein the cardiovascular disease is selected from the group consisting of myocarditis, cerebrovascular accident, mitral valve regurgitation, hypotension, arterial or post-transplantational atherosclerosis, fibrosis, thrombosis, and platelet aggregation wherein the fibrotic or connective tissue related condition is selected from the group consisting of tissue remodeling following e.g. inflammation, endomyocardial and cardiac fibrosis, mediastinal fibrosis, idiopathy pulmonary fibrosis, pulmonary fibrosis, retroperitoneal fibrosis, fibrosis of the spleen, fibrosis of the pancreas, alcohol and non-aicohol related hepatic fibrosis (cirrhosis), fibromatosis, uterine fibroids, angiofibroma, granulomatous lung disease, glomerulonephritis, endometrial fibrosis and endometriosis, diabetes related wound fibrosis, iymphangiogenesis, fibrodysplasia ossificans progressive, osteomyelitis, scar keloid, warts, synovitis, osteophyte, pannus growth, peritoneal sclerosis, ascites, hemophilic joints, and myelofibrosis. 14. A nucleotide sequence encoding the peptide according to claim 1. 15. A nucleotide sequence according to claim 14 wherein the sequence is set forth in SEQ ID NO: 23, or a degenerative variant thereof.