Size-Controlled MacromolQcule BACKGROUND OF THE INVENTION a) Field of the Invention The present Invention relates to the field of hyperbranched macromolecules. The present invention relates to the field of functionalized substrates on which is bound the macromolecules. The present invention also relates to the field of functionalized size-controlled dendrimers and dendrons that are used to bind to a functionalized substrate at one end of the dendron and to a target-specific ligand on the other end. The present invention also relates to the field of combinatorial chemistry, specific protein detection methods, specific nucleic acid or nucleic acid/peptide hybrid detection methods using a functionalized substrate to which is bound a hyperbranched polymer linked to a probe biomolecule. b) Description of the Related Art Since the first report (Fodor et al., Nature 364, 555-556 (1993); Saiki et al., Proc. Matt. Acad. Sd. USA 86,6230-6234 (1986)). DMA mteroarrays have attracted a great deal of attention because they allow high-throughput analysis of the DMA sequence, genetic variations, and gene expression. It is known that this methodology requires improvement in terms of fidelity, reprodudbHtty, and spot homogeneity that are essential for the standardization and application to human gene diagnosis (Hackett et al., Nature Biotechnology 21, 742-743 (2003)). These shortcomings are caused mainly by the variations in the nature of the surface and molecular interiayer structures that are far from ideal. Likewise, the field of high-throughput target detection systems encompasses bioassays utilizing immobilized bioactive molecules and biomolecules. Here we show that DMA micro-arrays fabricated on a nanoscale-controlled surface discriminates single mismatched pairs as effectively as DMA does in solution. This approach provides an ideal DNA-microarray in which each probe DNA strand is given ample space enough to interact with an incoming target DNA with minimal steric hindrance. The dramatically increased discrimination efficiency promises the very reliable diagnosis of human genes. Moreover, the approach is general enough to be applied to various bioassays utilizing immobilized bioactive molecules and biomolecules. Affinity purification is a well-known technique for the separation and identification of ligand-binding proteins (Cuatrecasas et al., Proc. Natl. Acad. Sci. U.S.A. 1968, 61, 636-643). A unique interaction between a ligand covalently attached to an insoluble matrix and the complementary target protein provides the specificity required for the isolation of biomolecules from complex mixtures. However, its widespread use has been hampered by the limited choice and instability of conventional matrices. Significant nonspecific binding of proteins to many solid supports has been a persistent problem in establishing new matrices (Cuatrecasas, P. J. Biol. Cham. 1970, 245, 3059-3065). It is therefore desirable to find new matrices that are comparable to the traditional matrices In terms of the specificity while exhibiting environmental stability and capability of well-defined and facile attachment of ligands. Aminopropyi-controlled pore glass (or AMPCPG) that is originally used for the solid-phase peptide synthesis appears to have many desirable features. However, the controlled pore glass (or CPG) surface is polar and retains partial negative charge even when coated (Hudson, D. J. Comb. Chem. 1999, 1,403-457). The feature plays a key role in significant nonspecific binding of proteins. Therefore, application on both affinity chromatography and solid-phase peptide synthesis has been limited. Once the obstacles are eliminated, widespread use of the materials can be expected. Accessibility of ligands is a key factor in determining binding capacity. The traditional approaches are introducing a spacer molecule and increasing the ligand concentration for better exposition of the ligand on the surface (Rusin, et al., Biosensors & Bioelectronlcs 1992, 7, 367-373; Suen et al., /rid. Eng. Chem. Res. 2000, 39,478-487; Penzol et al., Biotechnol and Bioeng. 1998, 60,518-523; Spinke et al., J. Chem. Phys. 1993, 99, 7012-7019). The approach works to a certain degree, but insufficient space between the ligands and random distribution of capture molecules over the surfaces are the issues yet to be solved (Hearn et al., J. Chromatogr. A. 1990, 512, 23-39; Murza et al., J. Chmmatogr. B. 2000, 740, 211-218; Xiao et al., Langmuir 2002, 18, 7728-7739). By far two methods have been employed to improve these shortcomings. One way is to utilize a big molecule such as protein as a placeholder. The protein is conjugated onto the matrix, and the placeholder molecule was cleaved off and washed out In this way, certain distance between the linkers left on the matrix is secured. Nevertheless, choice of the placeholder molecule and design of the deprotection route have to be elaborately optimized for every different situation (Hahn et al., Anal. Chem. 2003, 75, 543-548). Another way is to employ a cone-shape dendron that gives a highly ordered self-assembled monolayer and utilize an active functional group at the apex of the dendron (Xiao et al., Langmuir 2002, 18, 7728-7739; Whitesell et al., Langmuir 2003,19, 2357-2365). Here we present modification of AMPCPG with dendrons, further attachment of GSH at the apex of the dendrons, and characteristics of the surface materials in terms of GST proteins binding. A dendron featuring three or nine carboxylic acid groups at the termini and one amine group at the apex has been introduced into the matrices. Their carboxylic groups were covalently linked with the solid surface. Due to wide use and understating of glutathione S-transferase (or GST) gene fusion system, glutathione was chosen as a ligand to be tethered on the dendron-treated matrix. Ligand binding property of the matrix has been investigated with GST and two fusion proteins (GST-PX*7, GST-Munc-18) (Smith et al., Gene 1988, 67, 31-40; Sebastian et al., Chmmatogr. B. 2003, 786, 343-355; Wu et al., Chmmatogr. B. 2003, 786,177-185; De Carlos et al., J. Chmmatogr. B. 2003, 786, 7-15). SUMMARY OF THE INVENTION The present invention provides a substrate bound thereon size-controlled, preferably cone shaped molecules linked to a ligand. The present invention is directed to a substrate comprising a molecular layer of regularly spaced size-controlled macromotecules comprising a polymer comprising branched and linear regions in which a plurality of termini on the branched region are bound to the substrate, and a terminus of the linear region is functionalized. On the substrate, the macromolecules may be spaced at regular intervals. In particular, the macromolecules may be spaced at regular intervals between about 0.1 nm and about 100 nm between the linear functionalized groups. In particular, the macromolecules may be spaced at regular intervals of about 10 nm. In the above-described substrate, the terminus of the branched region may be functionalized with -COZ, -NHR, -OR1, or -PR"3, wherein Z may be a leaving group, wherein R may be an alkyl, wherein R' may be alkyl, aryl, or ether, and R" may be H, alkyl, alkoxy, or 0. In particular, COZ may be ester, activated ester, acid halide, activated amide, or CO-lmiazoyl; R may be CrC4 alkyl, and R' may be CrC4 alkyl. Further, in the above described substrate, the polymer may be a dendron. Still further, the linear region of the polymer may be comprised of a spacer region. And the spacer region may be connected to the branched region via a first functional group. Such first functional group may be without limitation -NH2l -OH, -PH3, -COOH, -CHO, or -SH. Still further, the spacer region may comprise a linker region covalently bound to the first functional group. In the substrate described above, the linker region may comprise a substituted or unsubstituted alkyl, alkenyi, alkynyl, cydoalkyl, aryl, ether, polyether, ester, or aminoalkyl group. Still further, spacer region may comprise a second functional group. The second functional group may include without limitation -NH2l -OH, -PH3, -COOH, -CHO, or -SH. The second functional group may be located at the terminus of the linear region. And a protecting group may be bound to the terminus of the linear region. Such protecting group may be acid labile or base labile. In another embodiment of the invention, in the substrate as described above, a target-specific ligand may be bound to the terminus of the linear region. In particular, the target-specific ligand may be a chemical compound, DNA, RNA, PNA, aptamer, peptide, polypeptide, carbohydrate, antibody, antigen, btomimetics, nudeotide analog, or a combination thereof. Further, the distance between the target-specific ligands bound to the linear region of the macromolecules may be from about 0.1 to about 100 nm. In yet another embodiment of the invention, the substrate described above may be made of semiconductor, synthetic organic metal, synthetic semiconductor, metal, alloy, plastic, silicon, silicate, glass, or ceramic. In particular, the substrate may be without limitation a slide, particle, bead , micro-well, or porous material. The porous material may be a membrane, gelatin or hydrogel. And further in particular, the bead may be a controlled pore bead. The Invention is also directed to a method for manufacturing a molecular layer of regularly spaced size-controlled macromolecules comprising a polymer comprising branched and linear regions In which a plurality of termini on the branched region are bound to the substrate, and a terminus of the linear region is functionalized, comprising: (i) functionalizing the substrate so that it will react with the termini of the macromoiecules; and (ii) contacting the macromoiecules to the substrate so that the termini and the substrate form a bond. In this method, the substrate may be made of without limitation semiconductor, synthetic organic metal, synthetic semiconductor, metal, alloy, plastic, membrane, silicon, silicate, glass, or ceramic. The substrate may be a slide, bead, microwell, or porous material. The porous material may be a hydrogel, gelatin, or membrane. The bead may be a controlled pore bead. Further, in the method described above, a target-specific ligand is fixed to the terminus of the linear region, comprising the steps of i) removing protecting group from the terminus of the linear region of the macromoiecules on the substrate; and ii) contacting the target-specific ligand or a linker molecule linked to the target-specific ligand to the terminus of the linear region of the macromoiecules on the substrate so that the ligand or the linker molecule and the terminus form a bond, wherein the linker molecule is a homobtfundional or heterobifunctional linker. In this method, the presence of the macromotecutes on the substrate results in minimal interference in the binding of the target-specific Hgand to the linear termini. Further in this method, the presence of the macromoiecules on the substrate results hi minimal interference in the detection of a target specific to the target-specific ligand. Still further, the target-specific llgand may be spaced at regular intervals. In particular, the target-specific llgands may be placed on the substrate at a low density. In the above-described method, the target-specific ligand may be a chemical compound, DNA, RNA, PNA, aptamer, peptide, polypeptide, enzyme, carbohydrate, polysaccharide, antibody, antigen, biomimetics, nudeotide analog, or a combination thereof. In another embodiment, the invention is also directed to a diagnostic system for detecting a mutation in a gene, comprising the above-described substrate, wherein the terminus of the linear region is fixed with target specific oligonucleotides. Such oligonucleotides may be specific for cancer related genes. In particular, the cancer related gene may be p53. In still another embodiment, the invention is directed to a method for detecting presence of a mutation in a gene, comprising contacting the above- described substrate with a sample containing the gene to be assayed, wherein the terminus of the linear region is fixed with a target specific oligonucleotide. In this method, the gene may be a cancer related gene. Further, the gene may be p53. These and other objects of the invention will be more fully understood from the following description of the invention, the referenced drawings attached hereto and the daims appended hereto. BRIEF DESCRIPTION OF THE DRAWINGS The present invention will become more fully understood from the detailed description given herein below, and the accompanying drawings which are given ty way of illustration only, and thus are not limitative of the present invention, and wherein; FIGURE 1 shows Formula I, which is a branched/linear polymer or a size-controlled macromotecute. FIGURE 2 shows a reaction scheme for producing a dendron. X represents a protecting group. FIGURES 3a-3c show detection of a dendron-modlfted surface. Fig. 3a shows a scheme for surface modification and hybridization. Fig. 3b shows the molecular structure of the employed dendron. Fig. 3c shows the DNA sequence of the probe and target DNA strands. Probe t«goriucleotides inck*Je Prc4» 1:5f-NH2-Ce-CAT TCC GNG TGT CCA-3' (SEQ ID NO:1) and Probe 2: 51-NHr Ra) is connected to a second generation group of branches RH (Rn, R12, RIS, R R22, Ra, RSI, Rs2, Rsa) by a functional group, W. The second generation group of branches is connected to a third generation group of branches RXXX (Rl11> R.112F Rl13. Rttl, Rl22i Rl23i R-131. Rl82. Rl33, R211. Ra2 RaS. Ra21, Rz22. Rz23. Rza. Raz Rzss Rani Ra2 Raw, Rs2 Rs22 Ra231 Raai. Ra32 RSSS) by a functional group W. And further fourth generation may be connected to the third generation branches in like fashion. The terminal R group is functionalized so that it Is capable of binding to the substrate. The R groups of all generations may be the same or different Typically, the R group may be a repeating unit, a linear or branched organic moiety, such as but not limited to alkyl, alkenyl, alkynyl, cydoalkyl, aryl, ether, polyether, ester, aminoalkyl, and so on. However, it is also understood that not all of the R groups need to be the same repeating unit. Nor do all valence positions for the R group need be filled with a repeating unit For Instance, in the first generation branch, Rx, Rii Ra. Rs all of the R groups at this branch level may be the same repeating units. Or, Ri may be a repeating unit, and R2 and RS may be H or any other chemical entity. Or, R2 may be a repeating unit, and RI and RS may be H or any other chemical entity. Likewise, for the second and third generation branches, any R group may be a repeating unit, H or any other chemical entity. Thus, a variety of shapes of polymers may be made in this way, for instance, if Rt, Rn, R«i, Rm and R113 are the same repeating units, and afl other R groups are H's or any number of small neutral molecule or atom, then a fairly long and thin polymer having a branch with three functional group termini for Rm, Rm and R113 is made. A variety of other optional chemical configurations are possible. Thus, it is possible to obtain from about 3 to about 81 termini having a functional group capable of binding to a substrate. A preferable number of termini may be from about 3 to about 75, from about 3 to about 70, from about 3 to about 65, from about 3 to about 60, from about 3 to about 55, from about 3 to about 50, from about 3 to about 45, from about 3 to about 40, from about 3 to about 35, from about 3 to about 30, from about 3 to about 27, from about 3 to about 25, from about 3 to about 21, from about 3 to about 18, from about 3 to about 15, from about 3 to about 12, from about 3 to about 9, or from about 3 to about 6. T-Terminal Group Terminal groups, T, are functional groups that are sufficiently reactive to undergo addition or substitution reactions. Examples of such functional groups include without limitation amino, hydroxyl, mercapto, carboxyl, alkenyl, allyl, vinyl, amido, halo, urea, oxlranyl, aziridinyl, oxazolinyl, imidazolinyl, sulfonato, phosphonato, isocyanato, isothtocyanato, silanyl, and halogenyl. W-FuncBonal Group In Formula I in Figure 1, W may be any functional group that may link a polymer to another (or any other divalent organic moiety), such as but not limited to ether, ester, amide, ketone, urea, urethane, imide, carbonate, carboxylic acid anhydride, carbodiimide, imine, azo group, amidine, thiocarbonyl, organic sulphide, disulfide, polysulfide, organic sulphoxide, sulphite, organic sulphone, sulphonamide, sulphonate, organic sulphate, amine, organic phosphorous group, alkylene, alkyleneoxlde, alkyleneamlne and so on. L - Spacer or Linker Group In Figure 1, the linear portion of the polymer may include a spacer domain comprised of a linker region optionally Interspersed with functional groups. The linker region may be comprised of a variety of polymers. The length of the linker may be determined by a variety of factors, including the number of branched functional groups binding to the substrate, strength of the binding to the substrate, the type of R group that is used, in particular, the type of repeating unit that is used, the type of the protecting group or target specific Bgand that is to be attached at the apex of the linear portion of the polymer. Therefore, it is understood that the linker is not to be limited to any particular type of polymer or of any particular length. However, as a general guideline, the length of the linker may be from about 0.5 nm to about 20 nm, preferably, about 0.5 nm to about 10 nm, and most preferably about 0.5 nm to about 5 nm. The chemical construct of the linker may include without limitation, a linear or branched organic moiety, such as but not limited to substituted or unsubstituted alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyi, aryl, ether, polyether, ester, aminoalkyl, polyalkenylglcol and so on. The linker may further include functional groups such as those described above, and as such is not limited to any particular structure. The linker group functionalized at the tip may comprise a protective group. Thus, in one aspect, the present invention Is directed to a substrate to which is attached a plurality of branched/linear polymers comprising linear tip attached to a protective group. Such a substrate may be chemically reacted to strip off the protective group to be replaced with a target specific ligand. Therefore, in a functional use of the present inventive system, a substrate bound with a population of branched/linear polymers Hnked to a library of target specific ligands is provided. X - Protecdna Group The choice of protecting group depends on numerous factors such as the desirability of acid-labile or base-lability. Therefore, the invention is not limited to any particular protecting group so long as it serves the function of preventing the reaction of the functional group to another chemical entity, and that it is capable of being stripped under desired specified conditions. Preferably, the protecting group is easily stripped away. Examples of such protecting groups that may be used in the present invention include without limitation the following: Amlno acid protecting groups: Methyl, Formyl, Ethyl, Acetyl, t-Butyl, Anisyl, Benzyl, Trifluroacetyl, N-hydroxysucdnimlde, t-Butyloxycarbonyl, Benzoyl, 4-Methylbenzyl, Thioanizyl, Thtocresyl, Benzyloxymethyl, 4-Nitrophenyl, Benzyk)xycarbonyl,2-Nitrobenzoyl, 2-Nitrophenylsulphenyl, 4-Toluenesulphonyl, Pentafluorophenyl, Diphenylmethyl (Dpm), 2-Chbrobenzyloxycarbonyl, 2,4,5-trichtorophenyl, 2-brornobenzyloxycarboriyl. 9-FkK>renvlmethyk»cycarbonyl, Triphenylrnethyl, 2^,5,7,8-oentanietriyl-chroman-6-sulphonvl, Phthatoyl, 3-NHrophthatoyl, 4,5-dichtofOphthatoyl, tetrabromophthaloyl, tetrachtorophthaloyl. Protecting groups for alcohols: p-Anisytoxymethyl (p-AOM), Benzytoxymethyl (BOM), t-Butoxymethyl, 2-ChJorotetrahvdrofuran (THF), Guaiacolmethvl (GUM), (1R)-Menthoxymethyl (MM), p-Methoxybenzytoxymethyl (PMBM), metoxyethoxymethyl (MEM), Methoxymethyl (MOM), o-Nitrobenzyloxymethyl, (Phenyldimethylsilyl)methoxymethyl (SMOM), 2-(Trimethylsilyl)ethoxymethyl (SEM). DNA, RNA protecting reagent: 2'-OMe-Ac-C-CE Phosphoramidite, 2'-OMe-Ac-RNA CPG, 2-OMe-l-CE Phosphoramidite, Z-OMe-S-Me-C-CE Phosphoramidite, Ac-C-CE Phosphoramidite, Ac-G-RNA 500, dmf-dG-CE Phosphoramidite, dmf-dG-CPG 500, 2-Amino-dA-CE Phosphoramidite, (M.P. Reddy, N.B. Hanna, and F. Farooqui, Tetrahedron Lett., 1994, 35,4311-4314; B.P. Monia, et al., J. Blol. Chem., 1993,268,14514-14522). Common Protecting Reagents in Organic Syntheses: (Dimethyl-t-butylsilyloxy)methyl chloride (SOMCI), Ethoxyethyl chloride (EECI), -chloro ethers, o-Nitrobenzyloxymethyl chloride, b.b.b-Trichloroethoxymethyl chloride (TCEMCI), (-)-Menthyl ester, (P)-Benzyl ester, 1,1,1,3,3,3-Hexafluoro-2-phenyl-2-propyl ether, 1,1,3,3-Tetramethyl-1,3t2-disilazane, 1,2,4-Dithiazolidine-3,5-dione, 1,2-Dibromlde, 1,2-Dichloride, 1,2-Diol mono-4-methoxybenzyl ether, 1,2-Diol mono-t-butyl ether, 1,2-Diol monoacetate ester, 1,2-Diol monoallyl ether, 1,2-Diol monobenzoate ester, 1,2-Diol monobenzyl ether, 1,2-Diol monotosylate, 1,3-Benzodithiolan, 1,3-Benzodithiolan-2-yl ether, 1,3-Dlol mono-4-methoxybenzyl ether, 1,3-Diol monobenzoate ester, 1,3-Diol monobenzyl ether, 1,3-Dioxan, 1-(2-(Trimethoxysilyl)ethoxy)ethyl ether, 1-Adamantyl ester, 1-Benzoyl-1-propen-2-yl amine, 1-Ethoxyethyl ether, 1-Methoxyethylldene acetal, 1-Methyl-1-methoxyethyl ether, 1-Phenyl-3,5-di-t-butylcyclohexadien-4-ony1 amine, 1-Phenylethyl ester, 2,2,2-Trichtoroethoxymethyl ether, 2,2,2-Trichloroethyl carbonate, 2,2,2-Trichtoroethyl ester, 2,2,2-Trichloroethyl phosphate, 2,2,5,7,8-Pentamethylchroman-6-sulphonamide, 2,2-Dimethyl-4-pentenoate ester, 2,3,6-Trimethyl-4-rnethoxybenzenesulphonamide, 2,4,6-TrimethylbenzenesulphonamkJe, 2,4-DNP hydrazone, 2,5-Dichlorophenyl phosphate, 2,5-Dimethylpyrroie, 2-(2-Methoxyethoxy)ethyl ester, 2-(4-Nitrophenyl)ethyl ether, 2-(4-Nitrophenyl}ethyl phosphate, 2-(4-Toluenesulphonyl)ethyl ester, 2- 20 %), which represents the degree of variation among the spots, and non-uniform fluorescence intensity within each spot On the other hand, PDITC linker assured better coefficient variance (CV) value (< 15 %) and homogeneous fluorescence intensity within a single spot like those of the dendron-modified substrate with DSC linker (Rg. 7). For additional comparison, probe 2 oNgonucleotides having an extra (T)x spacer at the 5* end of oligomer were utilized for SNP discrimination test. For this case, the probe with the extra spacer was immobilized on an APDES-modifled surface. The observed MM/PM ratios for T:T, G:T, and C:T cases were 0.17, 0.18, and 0.12 (Rg. 6d and Table 2). The selectivity was significantly enhanced in comparison with the case of probe DNA with a Ce spacer, but still was largely inferior to the dendron-modified DNA microarray. Hybridization on the surface poses various complications, hurdles to control and predict the microarray's screening performance precisely. Non-specific binding, steric and electrostatic effects, and environmental changes during the washing process should be considered in addition to the melting temperature (Tm) of the duplex and the Gibbs free energy for the duplex formation. Difference between the Gibbs free energy of the irrtemaknisrnatched pairs (T:T, G:T, and C:T internal mismatches of the 15-mer) and that of the perfectly matched pair in solution is 2.67, 1.75, and 3.05 kcal/moi at 50 °C. Gibbs free energy was calculated with HY-THER™ Software (http://ozone2.chem.wayne.edu). Therefore, the theoretical fluorescence ratios (MM/PM) are 0.016, 0.065, and 0.009 respectively. Also, study in solution phase with a molecular beacon showed that SNP discrimination ratio was as low as 1:0.01 (Taton et al., Science 289, 1757-1760 (2000)). These data strongly demonstrate that our dendron-modified DNA microarray represents an ideal case that reaches or even surpasses the thermodynamic limit In particular, for the G:T case, the discrimination efficiency in the microarray format is better than the value calculated for the solution phase. The answer to which factors are main reasons for the selectivity increase is yet to be investigated, but washing stringency may play a role. P53 SNP Detection In biological systems, the p53 tumor-suppressor gene plays key roles in cell regulation, gene transcription, genomic stability, DNA repair, and apoptosis (see Velculescu et al, 1996, Clin. Chem., 42: 858-868, Harris et al, 1996, 88:1442-1455, Sidransky et al, Annu, Rev. Med., 1996,47:285-301). It has been reported that loss of wild-type function of p53 can lead to cancer and p53 mutations are the most frequent genetic changes in human cancer such as colon, and lung cancer (GreenWatt, 1994, 54:4855-4878). DNA microarrays on [9]-acid dendron modified substrates were applied to the detection of single mutation of p53 tumor suppressor gene in cancer cell line. Target DNA samples (-200-400 bases) which contain 175 codon were prepared by random priming the genomic DNA templates and allowed to hybridize with dendron-modffied substrates on which 18mer probe oligonudeotides had been immobilized in a 10 by 1 format. The MM/PM ratio for A:C, T:C, and C:C internal mismatches were 0.028, 0.031, and 0.007 (Rg. 8a). This result shows that the outstanding selectivity holds for real target DMAs. The DNA microarrays on [27]-add dendron modified substrates were prepared using the same method as in the case of [9]-acid dendron which is described above and applied to the detection of single mutation of 175 codon of p53 tumor suppressor gene. The MM/PM ratio for A:C, T:C, and C:C internal mismatches were 0.066, 0.01, and 0.005 (Fig. 8b). This result indicates that the DNA microarrays on [27]-add dendron modified substrates also show outstanding selectivity for the detection of single mutation of real target DMAs. Detection of 7 hot soot mutations of o53 gene using single dendron-modlfied surface. The dendron-modified substrates were applied to the detection of single mutation of p53 tumor suppressor gene in cancer cell line. Target DNA samples (200-400 mer) which span 7 hot spot codons (175, 215, 216, 239, 248, 273, and 282) were amplified from the DNA extracted from cancer cells by random priming and allowed to hybridize with capture probes (oligonudeotides of 15-25 mer) corresponding to 7 hot spot codons that had been immobilized (Rgs. 9a and 9b). Excellent SNP discrimination efficiency was obtained. We fabricated successfully DNA microarray of the highest fidelity by providing mesospacing among the probe DNA, and found that SNP discrimination efficiency could be enhanced to reach or even surpass the solution value. The observed discrimination efficiency will make this methodology widely acceptable for very reliable high throughput gene diagnosis. It is expected that this strategy can be applied to various bioassays utilizing Immobilized biomolecules. Controlled Pore Glass Bead Natural polymers such as dextran and agarose are the most frequently used chromatography supports for affinity chromatography. Sepharose 6B, 4B, and 2B are chromatographic materials composed of cross-linked agarose, which exhibit extremely low nonspecific adsorption. In spite of their wide use, agarose gel, typically in a bead shape, suffers some drawbacks. For instance, the flow (or elution) rates are moderate due to their soft nature, they cannot be dried or frozen since they shrink severely and essentially irreversibly, and they do not tolerate some organic solvents (Cuatrecasas, P. J. Bfo/. Chem. 1970, 245, 3059-3065; Kim et al., Biochemistry 2002, 41, 3414-3421). In comparison, controlled pore glass (CPG) exhibits many exceptional properties for the support 1) it is mechanically stable, 2) it has a fixed three dimensional structure; it does not swell or shrink upon change of environment, 3) it is chemically stable from pH 1 to pH 14, 4) it is inert to a broad range of nucleophiiic and electrophilic reagents, 4) it is stable against heating, 5) it exhibits excellent flow (or elution) properties, 6) it shows less tendency to adhere to surface of containers. In addition, after a modification step, removal of reagents and byproducts through washing is rapid and efficient Al of these characteristics support potential usefulness in many fields such as permeation chrcfnatography, sofld phase synthesis, affinity purification, and so on. Pore size: Effective porosity of CPG toward an adsorbed molecule is determined by the accessfcity of the guest to the host surface. To a first approximation, the accessibility of CPG to a guest depends on geometric factors, which are related to the relative size of the pores of the host compared to the size of the guest. If a guest has a molecular size that Is larger than the pore openings leading to the internal surface, adsorption and interactions can only occur with the external surface, which is much smaller than the internal surface area of the investigated porous materials (Poschalko et al., J. Am. Chem. Soc. 2003, 125, 13415-13426; Ottaviani et al., J. Phys Chem. B. 2003, 707, 2046-2053). From these considerations, the extent and strength of adsorption of a guest onto CPG is expected to depend on the following parameters: pore size of CPG, the total surface area of the host, and the chemical composition of accessible surface of the host. In our investigation, three kinds of GST fused protein (GST (28 kDa), GST-PXP4T (41 kDa), and GST-Munc18 fragment (98 kDa)) were employed. Molecular dimension of GST-Munc18 should be similar to that of a fused GST of 100 kDa, GST-DREF (140x140x93 A3) (Hirose et al., J. Blol. Chem. 1996, 271, 3930-3937; Zhan et al., Gene 2001, 218, 1-9). To achieve the balance between pore size and surface area, porosity of the support has to be optimized for each specific protein. Because it is known that CPG with a pore size of approximately 50 nm allows the inclusion of complexes of the complete range of molecular subunits normally found in proteins our investigation had been carried out with 50 nm CPG. Simultaneously, use of CPG with a larger pore (300 nm) confirmed the effectiveness of the former CPG as far as the above proteins are concerned (Collins et al., Anal. Blochem. 1973, 54,47-53; Halter, W. J. Chromatogr. 1973, 85,129-131). Modification of Glutathlone CPG (Sample E1, E3, A, CS, and CL): A key concern of affinity matrices is degree of nonspecific binding (or NSB). It is a ubiquitous problem in affinity purification and solid-phase synthesis. In general, key factors to suppress nonspecific binding are to avoid the hydrogen bond donor groups and increase the hydrophilidty of matrices (Sigal et al, J. Am. Chem. Soc. 1998, 120, 3464-3473; Chapman et al., Langmuir 2000, 16, 6927-6936; Chapman et al., J. Am. Chem. Soc. 2000, 122,8303-8304; HoJmlin et al., Langmuir 200^, 17, 2841-2850; Ostuni et al., Langmu/r 2001,17,6336-6343; Chapman et al., Langmuir 2001, 17, 1225-1233; Ostuni et al., Langmu/r 2001, 17, 5605-5620). CPG surface, even when modified with an aminoatkyl group, is polar and retains partial negative charge (Hudson, D. J. Comb. Chem. 1999, 1, 403-457). Use of a diepoxide as a spacer had been reported to be responsible for the hydrophiBc character of the matrix and the minimal nonspecific binding (Suen et al., Ind. Eng. Chem. Res. 2000, 39, 478-487; Sundberg et al., J. Chromatogr. B. 1974, 90, 87-98; Shimlzu et al., Nature Biotechnology 2000,18, 877-881). Therefore, 1,4-butanediol diglycldyl ether (or BUDGE) was employed for the modification leading to sample E1 and E3. The key features of the incorporation of BUDGE include generation of very stable ethereal bond against hydrolysis, the enhanced flexibility through a long spacer arm, full distance from the surface, and suppression of nonspecific binding to a certain extent. The last advantage can be explained by resembled structural motif with that of polyethylene glycol. Diepoxides can be utilized to link a molecule and a surface having a nudeophile, such as amine and thiol. During the ring opening process, stable carbon-heteroatom bond is generated as well as a B-hydroxy group. Use of the linker before and after dendron modification guarantees flexibility of the tethered GSH. The summarized modification steps are outlined In Figure 10. For incorporation of the dendrons on the matrices, common reagents called EDC and NHS were used. After modification with the dendrons, acetic anhydride was introduced into system to cap the remained amine functionality. Finally, matrices were treated by 20 % piperidine for 30 min to deblock the Fmoc group of the dendrons for the further modification. After elongation with BUDGE one more time, GSH was immobilized by utilizing reaction between the thlol and the epoxide. As a control, sample A was prepared. Sequential modification with BUDGE, 1,3-diaminopropane, and BUDGE gave surface materials that is exactly same as E1 and E3 except absence of the dendrons. As before, GSH was immobilized by ring opening reaction between the epoxide and the thiol. Other control beads (Sample CL and CS) were prepared by using a heteroblofunctional linker called GMBS to link GSH and AMCPG or LCAA-CPG. While, AMPCPG has a short arm consisting C3 hydrocarbon at the surface, LCAA-CPG has a long arm of C15 aliphatic chain. After amide formation with GMBS was allowed, the beads were treated with GSH. Addition of thiol group into maleimkJo group generated a covalent bond between carbon and sulfur atoms. The two-step treatment produced GSH immobilized controlled pore glass beads, i.e. CS and CL, with covalent bonds. Ugand Density Measurement: Due to the difficulties in measuring the amount of immobilized gkitathione directly, an indirect method that the Kgand density was determined by measuring amount of dibenzofurvene released during the deprotection step was employed. 9-Fluorenylrnethoxycarbonyl (Fmoc) protecting group at the apex of the dendrons is stable against adds but is readily cleaved by a variety of bases. In this study 20 % piperidine in DMF is employed to deprotect the Fmoc functional group. Piperidine forms an adduct with the dibenzofulvene, and the adduct absorbs at 301 nm (0ye et al., J. Phys. Chem. B. 2003, 107, 3496-3499). On the other hand, when the absorbance of the collected solution appeared at 301 nm during the deprotection step with 20 % piperidine, it indicated that the deprotection proceeded as intended. Ugand density obtained with this method is 8.3 i/mol/g for E1, 5.6 /imol/g for E3. The density is reduced by a factor of 11.1 upon modification with F-moc(3)acid and the value is further reduced by a factor of 1.5 upon use of a larger dendron. Thus, In a specific embodiment of the invention, smaller dendrons were more effective at obtaining higher density than using larger dendrons. GST Binding Assay. Binding characteristics of sample A, E1, and E3 were examined using purified GST and cell lysate (lane 2, 3, and 4 in Figure 11). Lane 1 shows successful preparation of lysate. It is evident that the three matrices bind purified GST effectively. When cell lysate was introduced into the beads (lane 5, 6, and 7), a significant difference was observed between A and E1 or E3. For sample A. in spite of incorporation of BUDGE linkers, serious nonspecific binding was observed. Interestingly, when the dendrons were introduced on the matrix, nonspecific protein binding was effectively suppressed. It is noteworthy that self-assembly of either the dendron of the first generation or the one of the second generation effectively suppresses nonspecific binding of the solid support, while an extended spacer between the dendron and GSH retains the activity of the tethered tripeptide. In Figure 12, in one aspect of the invention, etheral and amide groups constitute the main backbone of the structure, and immobilization of the dendrons generates again amide bonds. Also, high coverage of the dendrons is also an important factor for the success. The ligand density for E1 is 1.48 times higher than that for E3. In other words, 148 % of the ligand concentration was recorded for E1 (Table 3). In order to examine the binding efficiency of both beads, the weight of the samples was adjusted to have the same number of GSH in each sample. Densltometer showed that the Kgand utilization for both cases was quite dose (29 %, 31 %). The larger spacing of E3 does not enhance the binding efficiency of GST, probably because the examined protein is larger than the spacing of both E1 and E3 anyway. Table 3: Ligand concentration and ligand utilization of sample E1 and E3. (Table Removed) Control experiment: We found that density of GSH was 14.5 y^mol/g for CS, 11.9 //mol/g for CL. To compare efficacy of the beads in terms of specific binding of GST, captured proteins with CS (5.7 mg) and CL (7.0 mg) beads were analyzed along with samples from E1 (10.0 mg) and E3 (14.8 mg) beads. The utilized quantity was adjusted to have the same number of the GSH roughly. It is evident in the chromatogram (Figure 13) CS and CL beads display poor selectivity as well as low binding capacity. The result stresses again importance of the dendron to guarantee not only improved accessibility of GST towards immobilized GSH but effective suppression of nonspecific binding. Molecular Weight Dependence. Because the dendron modification generates a surface of controlled spacing between the immobilized ligands, binding capacity towards proteins of various molecular weights is intriguing. In particular, it is known that use of the second generation dendron guarantees a spacing over 24 angstrom (Cardona et al., J. Am. Chem. Soc. 1998, 120, 4023-4024). For this particular test, GST protein (28 kDa), GST-PX1*7 (41 kDa), and GST-munc-18 fragment (98 kDa) from the wild-type lysate were prepared. As shown in Rg. 14, binding capacity of the beads (E1, E3, and Sepharose 4B) decreases sharply as molecular weight of proteins increases. It is interesting to note that the degree of decrease holds same for the three different cases. When binding capacity of E1 is set at 100 % for GST, GST-PX1*7 has a relative biding capacity of 92% and 22 % for GST-munc18. For E3 bead, 85 % for former protein and 23 % for the latter protein are recorded. This strong dependence on protein molecular weight was also observed wtth gMathione Sepharose-4B. For glutathtone Sepharose-4B. the binding efficiencies are 104 % and 17 % for GST-PX**7 and GST-muncIS, respectively. The only notable Difference is a rather constant capacity for GST and GST-PX1*7 for this commerdatty available matrix. The difference might reflect heterogeneous spacing In Sepharose 4B. In this material, diverse spadngs between GSH exist so that the matrix binds the fused GST as efficiently as the pristine GST. For the much bigger protein, GST-munc18, the spadngs should be too small. In this regard, constant decrease of binding capacity of the dendron-treated beads supports again the regular spadng of GSH on the surface. In summary, the dendron-modified matrix demonstrates selectivity as high as that of the commercial matrix (for example, Sepharose 4B), and almost same molecular weight dependence as the commercial one. The incorporation of the dendrons on AMPCPG matrix not only reduces the nonspecific binding effectively, but retains binding activity of GSH. Constant decrease of the binding capacity as increase of protein molecular weight was observed, and the phenomenon seems in harmony with the regular spadng between the immobilized GSH. In addition to the well-controlled spacing, favorable aspects such as mechanical stability, wide compatibility with various chemical environment, and easiness to handle promise interesting applications. The present invention is not to be limited in scope by the specific embodiments described herein. Indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description and accompanying figures. Such modifications are intended to fall within the scope of the appended claims. The following examples are offered by way of illustration of the present invention, and not by way of limitation. EXAMPLES Numbering scheme is used for compounds throughout the Examples such as compound 1, compound 2, I, II, III, IV, V and so on. It is to be understood however, that the compound numbering scheme is consistent with and is confined to the particular Example section to which it Is recited. For instance, compound 1 as recited in Example 2 may not necessarily be the same compound 1 as found in Examples. Example 1 - Methods For Making Mteroarray Using Size-Controlled Macrotnolecule In Example 1, designations I, II, III, IV, and V refer to various compounds and Intermediate compounds as shown In Figure 2. Example 1.1 - Materials. The sllane coupling reagents, (3- glyddoxypropyl)methyldiethoxysilane (GPDES) and (3- aminopropyl)diethoxymethylsilane (APDES), were purchased from Gelest, Inc. and all other chemicals were of reagent grade from Slgma-AJdrich. Reaction solvents for the silylation are anhydrous ones in Sure/Seal bottles from Aldrich. All washing solvents for the substrates are of HPLC grade from Mallinckrodt Laboratory Chemicals. The UV grade fused silica plates (30 mm x 10 mm x 1.5 mm) were purchased from CVI Laser Corporation. The polished prime Si(100) wafers (dopant, phosphorus; resistivity, 1.5-2.1 Q«cm) were purchased from MEMC Electronic Materials, Inc. Glass slides (2.5 x 7.5 cm) were purchased from Coming Co. All of the oligonudeotides were purchased from Metabion. Ultrapure water (18 M Q/cm) was obtained from a Milli-Q purification system (Millipore). Example 1.2 - Instruments. The film thickness was measured with a spectroscopic ellipsometer (J. A. Woollam Co. Model M-44). UV-vis spectra were recorded on a Hewlett-Packard diodearray 8453 spectrophotometer. Tapping mode AFM experiments were performed with a Nanoscope Ilia AFM (Digital Instruments) equipped with an "E" type scanner. Example 1.3 - Cleaning the substrates. Substrates such as oxidized silicon wafer, fused silica, and glass slide, were immersed into Piranha solution (cone. H2SO4:30% H2O2 = 7:3 (v/v)) and the reaction bottle containing the solution and the substrates was sonicated for an hour. (Caution: Piranha solution can oxidize organic materials explosively. Avoid contact with oxidizable materials.) The plates were washed and rinsed thoroughly with a copious amount of deionized water after the sonication. The dean substrates were dried in a vacuum chamber (30-40 mTorr) for the next steps. Example 1.4 - Preparing the hydroxylated substrates. The above dean substrates were soaked in 160 ml toluene solution with 1.0 ml (3-glyddoxvpropyl)methykJiethoxysilane (GPDES) for 10 h. After the self-assembly, the substrates were washed with toluene briefly, placed in an oven, and heated at 110°C for 30 min. The plates were sonicated in toluene, tokiene-methanol (1: 1 (v/v)), and methanol in a sequential manner for 3 min at each washing step. The washed plates were dried in a vacuum chamber (30-40 mTorr). GPDES-modified substrates were soaked in a neat ethytene glycol (EG) solution with two or three drops of 95 % sulfuric acid at 80 -100 "C for 8 h. After cooling, the substrates were sonicated in ethanol and methanol in a sequential manner each for 3 min. The washed plates were dried in a vacuum chamber (30-40 mTorr). Example 1.5 - Preparing the dendron-modrfled substrates. The above hydroxylated substrates were immersed into a methylene chloride solution dissolving the dendron (1.2 mM) and a coupling agent, 1-[-3-(dimethylamino)propyl]-3- ethylcarbodiimide hydrochloride (EDC) or 1,3-dicydohexylcarbodiimide (DCC) (11 mM) in the presence of 4-dimethylaminopyridine (DMAP) (0.82 mM). After 3 days at room temperature, the plates were sonicated in methanol, water, and methanol in a sequential manner each for 3 min. The washed plates were dried in a vacuum chamber (30-40 mTorr) for the next step. Example 1.6 - Preparing the NHS-modlfled substrates. The dendron-modifled substrates were immersed into a methylene chloride solution with 1.0 M trifluoroacetic acid (TFA). After 3 h, they were again soaked in a methylene chloride solution with 20% (v/v) diisopropylethylamine (DIPEA) for 10 min. The plates were sonicated in methylene chloride and methanol each for 3 min. After being dried hi a vacuum chamber, the deprotected substrates were incubated in the acetonftrile solution with di(N-sucdnimidyi)carbonate (DSC) (25 mM) and DIPEA (1.0 mM). After 4 h reaction under nitrogen atmosphere, the plates were placed in a stirred dimethylformamide solution for 30 min and washed briefly with methanol. The washed plates were dried in a vacuum chamber (30-40 mTorr) for the next step. Example 1.7 - Arraying oligonucleotides on the NHS-modrfled substrates. Probe oligonucleotides in 50 mM NaHCOS buffer (pH 8.5) were spotted side by side in a 4 by 4 format on the NHS-modifled substrate. The mteroarray was incubated in a humidity chamber (80 % humidity) for 12 h to give the amlne-tethered DMA sufficient reaction time. Slides were then stirred in a hybridization buffer solution (2x SSPE buffer (pH 7.4) containing 7.0 mM sodium dodecylsuifate) at 37 °C for 1 h and in boiling water for 5 min to remove non-specifically bound oligonucleotides. Finally, the DNA-funcUonaHzed mteroarray was dried under a stream of nitrogen for the next step. For a fair comparison, different kinds of probes were spotted in a single plate. Example 1.8 - Hybridization. Hybridization was performed in the hybridization buffer solution containing a target oUgonudeotide (1.0 nM) tagged with a Cy3 fluorescent dye at 50 °C for 1 h using a GeneTACTM HybStation (Genorrtc Solutions, Inc.). The microarray was rinsed with the hybridization buffer solution in order to remove excess target oUgonudeotide and dried with nitrogen. The fluorescence signal on each spot was measured with a ScanArray Lite (GSI Lumonics) and analyzed by Imagene 4.0 (Biodiscovery). EXAMPLE 1.9 - Synthesis of the dendron EXAMPLE 1.9.1 • Preparation of 9-anthrylmethyl N-(3-carboxylpropyl)carbamate (I) - Compound I. 4-Aminobutyric acid (0.50 g, 4.8 mmol, 1.0 equiv) and triethylamine (TEA) (1.0 ml, 7.3 mmol, 1.5 equiv) were dissolved in N,N-dimethylformamide (DMF) and stirred at 50 °C. 9-Anthrylmethyl p-nitrophenyl carbonate (1.81 g, 4.8 mmol, 1.0 equiv) was slowly added while stirring. After stirring at 50 °C for 2 h, the solution was evaporated to dryness, and the solution was baslfied with 0.50 N sodium hydroxide (NaOH) solution. The aqueous solution was washed with ethyl acetate (EA), stirred in an ice bath and acidified with dilute hydrochloric acid (HCI). After the product was extracted with EA, the organic solution was dried with anhydrous MgSO4, filtered and evaporated. The total weight of the resulting yellow powder was 1.06 g and the yield was 65 %. 1H NMRfCDCIa) 5 11.00-9.00(br, CH2COOH, 1 H), 8.41 (s, d4H9CH2, 1 H), 8.31 (d, C14W8CH2l 2H), 7.97 (d, C14AfeCH2, 2H), 7.51 (t, C14H8CH2, 2H), 7.46(t, d^CH* 2H), 6.08(s, d4H8CHA 2H), 5.01 (t, OCONHCH2,1 H), 3.23(q, NHCHzCH* 2H), 2.34(t, CHzCHzCOOH, 2H), 1.77(m, CH2CH2CH2, 2H). 13C NMR(CDCI3) 6 178.5{CH2COOH), 157.9(OCONH), 132.1 (C14H9CH2), W.7(CHHeCHd, 129.7(C14H9CH2), 129.7(d4H9CH2), 127.3(C14H9CH2), 126.8(C14H9CH2), 125.8( d4H9CH2), 124.6( C14H9CH2), 60.2(C14H9CH2), 41.0(NHCH2CH2), 31.7(CH2CH2COOH),25.6(CH2CH2CH2). EXAMPLE 1.9.2 - Preparation of 9-anthrylmethyl N-{[(tris{[2-(methoxvcarbonyl)ethoxy]rnethyl}rnethy)) amlno]carbonyl}propylcarbonate (II) - Compound II. 9-Anthrylmethyl N-{3-carboxylpropyOcarbamate (0.65 g, 1.93 mmol, 1.5 equfv), 1-^3^dimethylamlr»)propyrj-3-ethykar^ hydrocnlorkJe (EDO) (0.37 g, 1.93 mmol, 1.5 equiv), and 1-hydroxybenzotriazote hydrate (HOBT) (0.261 g, 1.93 mmol, 1.5 equiv) were dissolved in acetonftrite and stirred at room temperature. Tris{[(metrK)xycarbonyl)ethoxyJrnetnyl} aminomethane (0.49 g, 1.29 mmol, 1.0 equiv) dissolved in acetonitrite was added with stirring, After stirring at room temperature for 12 h, the acetonitrile was evaporated. The crude product was dissolved in EA and washed with 1.0 N HCI and saturated sodium bicarbonate solution. After being dried with anhydrous MgSO4, filtered, and evaporated, the crude product was loaded in a column packed with silica gel. Purification by column chromatography (eluent ethyl acetate-.hexane = 5:1 (v/V)) resulted in a viscous yellow liquid. The total weight of the yellow liquid was 0.67 g, and the yield was 74 %. 1H NMR(CDCI3) 6 8.43(s, CuHoCHfc 1 H), 8.36(d, d^gCH^ 2H), 7.99 (d, d^CHa 2H), 7.53(t, d^CH* 2H), 7.47(t, d^CH* 2H), 6.15(s, CONHC, 1H), 6.08(s, C14H9CW2O, 2H), 5.44(t, OCONHCH2,1 H), 3.63-3.55(m, CH2OCH2CH2COOCH3, 21 H), 3.27(q, NHCH2CH2l 2H), 2.46(t, CH2CW2COOCH3, 6H), 2.46(t, CH2CW2CONH, 2H), 1.81 (m, CH2CH2CH2, 2H). 13C NMRCCDCIg) 6173.2(CH2CONH), 172.7(CH2COOCH3), 157.4(OCONH), 131.5(C14H6CH2), 129.5(C14H9CH2), 129.4(0,^,^2}, 127.5(C14H9CH2), 127.0(C14H9CH2), 125.6(d4H9CH2), 124.7(Ci4H9CH2), 69.6(NHCCH2O), 67.2(C14H9CH2), 60.1 (OCH2CH2), 59.4(NHCCH2), 52.1(OCH3), 40.8(NHCH2CH2), 35.1 (OCH2CH2), 34.7(CH2CH2CONH), 26.3(CH2CH2CH2). Anal. Gated for CwrtwNzOu 0.5 H2O: C 61.18, H 6.65, N 4.03; Found: C61. 09, H 6.69, N 3.96. EXAMPLE 1.9.3 - Preparation of 9-anthrylmethyl N-[({tris[(2-carboxyethoxy)methyl]methyl}amlno) carbonyljpropylcarbamate (III) -Compound III. 9-Anthrylmethyl N-{[(tris([2- (methoxycarbonyl)ethoxy]methyf}methyl)amino]carbonyl}propyl- carbonate (0.67 g, 0.93 mmol) was dissolved in acetone (30 ml) and 0.20 N NaOH (30 ml, 6 mmol). After being stirred at room temperature for 1 d, the acetone was evaporated. The aqueous solution was washed wtth EA, stfarred in an ice bath and acidified with dBute HCI. After the product was extracted with EA, the organic solution was dried wtth anhydrous MgSO4, filtered and evaporated. Solidification In acetone and ether solution at -20 °C resulted in a yellow powder. The total weight of the final pale yellow powder was 0.54 g wtth a yield of 88%. 'H NMR(CDCIs) 5 11.00-9.00(br, CHjjCOOH, 3H}, 8.61 (s, d^CH* 1H), 8.47(d, C14H9CH2, 2H), 8.11 (d, C14«9CH2, 2H), 7.60(t, Ci4HBCH2. 2H}, 7.52(t, C14H9CHz. 2H), 6.63(s, CONHC, 1 H), 6.36(t, OCONHCHa 1 H), 6.1 2(s, C^HoCHzO, 2H). 3.40-363(m, CH2OCW2CH2COOH, 12H), 3.20(q, NHCH2CH2, 2H), 2.52(t, CHzCHjCOOH, 6H), 2.17(t, CHzCH^ONH, 2H), 1.75(m, CHaCHzCH* 2H). 13C NMR(CDCIa) 6 172.2(CH2COOH), 172.0(CH2CONH), 156.7(OCONH), 131.2(0,^0^), 130.7(C14H9CH2), 128.6(C14HflCH2), 128.4(Ci4H9CH2), 127.3(C,4H9CH2), 126.2(C14H9CH2), 124.8(C14H9CH2), 124.0(Ci4H9CH2), 68.6(NHCCH2O), 66.5(C14H9CH2), 59.5(OCH2CH2), 58.0(NHCCH2), 40.0(NHCH2CH2), 34.0(OCH2CH2), 33.5(CH2CH2CONH), 25.8(CH2CH2CH2). Anal. Calcd for CasH^N^' 1.5 H2O: C 57.97, H 6.34, N 4.10; Found: C 57.89, H 6.21, N 4.09. EXAMPLE 1.9.4 - Preparation of 9-anthrytmethyl N-[({trls[(2-{[(trls{[2-(methoxycarfoonyl)ethoxy]m0ttiyl} (methyt)amim>]carix>nyl}ethoxy)methyl]methyl}amino)carbonyl]propylcarbam ate (IV) - Compound IV. 9-Anthrylmethyl NH;({tris[(2xyetrK>xy)me%Oniethy'}af"lno)carbonyl] propylcarbamate (0.54 g, 0.82 mmol, 1.0 equiv), EDO (0.55 g, 2.87 mmol, 3.5 equiv), and HOBT (0.39 g, 2.89 mmol, 3.5 equiv) were dissolved in acetonitrile and stirred at room temperature. Trisfl(methoxycarbonyl)ethoxy]methyl} aminomethane (0.96 g, 2.53 mmol, 3.1 equiv) dissolved in acetonitrile was added with stirring. After stirring at room temperature for 36 h, the acetonitrile was evaporated. The crude product was dissolved in EA and washed with 1.0 N HCI and saturated sodium bicarbonate solution. After drying with anhydrous MgSO4l filtered, and evaporated, the crude product was loaded in a column packed with silica gel. Column purification (eluent: ethyl acetate:methanol = 20:1 (v/v)) resulted in a viscous yellow liquid. The total weight of the yellow liquid was 1.26 g with an 88% yield. 'H NMRfCDCy 6 8.47(s. CwHfcCHa, 1 H), B.39(d, CuHfcCHz, 2H). 8.02 (d, C^CH* 2H), 7.53(t, d^CHz, 2H), 7.47(t, C^CH* 2H), 6.60(s, CHzCHzCHzCONHC, 1 H), 6.13(s, OCHzCHzCONHC, 3H), 6.11 (s, C^HoCHzO. 2H), 5.79(t, OCONWCrfcl H), 3.65-3.60(m, CHzOCHjCHzCONH, CHsQCH&HjCQOCH* 75H), 3.29(q, NHCHzCH* 2H), 2.50(t, CHjOfzCOOCH* 18H), 2.36(t, OCHjCHzCONH, 6H), 2.27(t, CH2CH2CW2CONH, 2H), 1.85(m, CH2CH2CH2,2H). 13C NMR(CDCI3) 6 173.3(OCH2CH2CONH), 172.5(CH2CH2CH2CONH), 171.6(CH2COOCH3), 157.2(OCONH), 131.8(C,4H8CH2), 131.5(d4H9CH2), 129.4(C14HeCH2), 129.3(C,4H9CH2), 127 .6(Ci4H9CH2), 127.0(Ci4H9CH2), 125.6(C14H9CH2), 124.7(C14H9CH2), 69.5(NHCCH2OCH2CH2COOCH3), 67.9(NHCCH20CH2CH2CONH), 67.2(01-^8^2), eo.S^CH^HzCONH), 60.2(OCH2CH2COOCH3), 59.2(NHCCH2OCH2CH2COOCH3, NHCCH2OCH2CH2CONH), 52.1(OCH3), 41.0(NHCH2CH2), 37.6(OCH2CH2CONH), 35.1(OCH2CH2COOCH3), 34.7(CH2CH2CH2CONH), 26.3(CH2CH2CH2). Anal. Calcd for CsiHi^NsOsB ' H^: C 55.31, H 7.05, N 3.98; Found: C 55.05, H 7.08, N 4.04. MALDI- TOF-MS: 1763.2 (MNa+), 1779.2 (MK+). EXAMPLE 1.9.5 - Preparation of 9-anthrylmethyl N-(fltris({2-[({trls[(2-carboxvethoxy)rnethyrjmethyr} amino)caiix>ny1]ethoxy}methy1)methy1]amino}caitK>ny1)propylcarbarnate (V) -Compound V. 9-Anthrylmethyl N-[({tris[(2-{[(tris{I2- (ir^trK5xycarbonyl)ethoxy]methyl}rnethyl)amino]carbonyl} ethoxy)methyl]methyl}amino)carbonyl]propylcarbamate (0.60 g, 0.34 mmol) was dissolved In acetone (30 ml) and 0.20 N NaOH (30 ml). After stirring at room temperature for 1 d, the acetone was evaporated. The aqueous solution was washed with EA, stirred in an ice bath and acidified with dilute HCI. After the product was extracted with EA, the organic solution was dried with anhydrous MgSO4l filtered and evaporated. The total weight of the final yellow powder was 0.37 g and the yield was 68 %. 1H NMR(DMSO) 6 13.00-11.00(br, CHjCOOH, 9H), 8.66(s, C14HbCH2, 1 H), 8.42(d, CwHgCHz, 2H), 8.13 (d, C,4>*CH2, 2H), 7.62(t CuAfcCH* 2H), 7.54(t, C^CH* 2H), 7.12(t, OCONHCH2, 1H), 7.10(s, OCHaCHzCONHC, 3H), 7.06(s, CHzCHaCH^ONHC, 1 H), 6.06(s, d^C/^O, 2H). 3.57-3.55(m, CHjOCHzCHzCONH, C^OCHzCHzCOOH, 48H), 3.02(q, NHCHzCHa, 2H), 2.42(t, CHzCHzCOOH, 18H), 2.32(t, CX^HzC^zCONH, 6H), 2.11(t, CHaCHaCHaCONH, 2H), 1.60(m,CH2CW2CH2,2H). 13C NMR(DMSO) 6 172.8(CH2COOH), 172.2(CH2CH2CH2CONH), 170.5(OCH2CH2CONH), 156.5(OCONH), 131.0(d4H9CH2), 130.6(d4HBCH2), 129.0(C14H9CH2), 128.7(C14H9CH2), 127.6(d4H9CH2), 126.7(C,4H8CH2), 125.4(Ci4H9CH2), 124.3(C14H9CH2), 68.3(NHCCH2OCH2CH2COOH), 67.4(NHCCH2OCH2CH2CONH), 66.8(Ci4H9CH2), 59.8(OCH2CH2COOH), 59.6(OCH2CH2CONH), 57.9(NHCCH2OCH2CH2CONH), 55.9(NHCCH2OCH2CH2COOH), 36.4(NHCH2CH2), 34.6(OCH2CH2COOH), 30.8(OCH2CH2CONH), 29.7(CH2CH2CH2CONH), 25.9(CH2CH2CH2). EXAMPLE 2 - Methods of producing alternative starting material dendron macromolecule - Fmoc-Spacer-[9]-acld In Example 2, various indicated compounds are referred to as compound 1, 2 and so forth. First, we synthesized a spacer, 6-azidohexylamine (1) from 1,6-dibromohexane according to Lee, J. W.; Jun, S. I.; Kim, K. Tetrahedron Lett., 2001, 42, 2709. NaN, Tripheaylphosphine *• N3X This spacer was attached to repeating unit (2) through unsymmetric urea formation and made Nrspacer-[3]ester (3). The repeating unit was synthesized by condensation of TRIS with terf-butyl acrylate, which had been reported in Cardona, C. M.; Gawtey, R. E. J. Org. Chem. 2002,67,141. (Figure Removed) This Wester was transformed to N3-spacer-[3]acid (4) through hydrolysis and coupled with Wester (2) under peptide coupling conditions, which led to Nr spacer-[9]ester. After reduction of azide to amine and protection of amine with Fmoc group, hydrolysis of nonaester afforded Fmoc-spacer-[9]add (5). (Figure Removed) methyfurea (3). Triphosgene (1.3 g, 4.3 rnrnol) was dissolved in anhydrous CHzda (20 ml). A mixture of 6-azWohexylamine (1) (1.6 g, 12 mmol) and N,N-diisopropytethylamine (DIEA, 2.4 ml_ 13.8 mmol) in anhydrous CHzda (35 mL) was added dropwise to the stirred solution of triphosgene over a period of 7h using a syringe pump. After further stirring for 2h, a solution of (2) (6.4 g, 13 mmol) and DIEA (2.7 ml, 15.2 mmol) in anhydrous CHs»C12 (20 ml) was added. The reaction mixture was stirred for 4 h at room temperature under nitrogen, and washed with 0.5 M HCI and brine. The organic layer was then dried over anhydrous MgSO4, and the solvent was removed by evacuation. Purification with column chromatography (silica, 1:1 EtOAc/hexane) yielded colorless oil (3.0 g, 40 %). 1H NMR (CDCIs, 300 MHz): 6 1.45 (s, (CH&C, 27H); 1.36-1.58 (m, CH2CHzCHzCH2, 8H); 2.46 (t, CHzCHA J = 6.4 Hz, 6H), 3.13 (m, CONHCH2, 2H), 3.26 (t, N3CH2, J = 6.9 Hz, 2H), 3.64-3.76 (m, CCH2O and ChfeCffcO, 12H); 5.00 (t, CH2NHCO, J=6.7 Hz, 1H), 5.29 (s, CONHC, 1H). 13C NMR (CDCI3, 75 MHz): 6 26.52, 26.54, 28.81, 30.26 (CH2CH2CH2CH2); 28.14((CH3)3C); 36.20 (CH2CH2O); 39.86 (CONHCH2); 51.40 (NaCHz); 58.81 (CCH20); 67.16 (CH2CH2O); 69.23 (CCHaO); 80.58 ((CH3)3C); 157.96 (NHCONH); 171.26(COOf-Bu). FAB-MS: 674.26 (M+). NK6-Azidohexy1)-M'-tris{[2-carboxyethoxy]methyl}methylurea (4). Ns- spacer-[3]ester (3) (0.36 g, 0.56 mmol) was stirred in 6.6mL of 96 % formic add for 24 h. The formic add was then removed at reduced pressure at 50 °C to produce colorless oil in a quantitative yield. 1H NMR (CD3COCD3, 300 MHz): 6 1.34-1.60 (m, CH2CH2CW2CH2, 8H); 2.53 (t, CH^HzO, J = 6.4 Hz, 6H), 3.07 (t, CONHCH2, J = 6.9 Hz, 2H), 3.32 (t, N3CW2, J = 6.9 Hz, 2H), 3.67-3.73 (m, CCHjP and CH2CHA 12H). 13C NMR (CD3COCD3, 75 MHz): 6 27.21, 29.54, 31.02 (CH2CH2CH2CH2); 35.42 (CHzCHzO); 40.27 (CONHCH2); 52.00 (NsCHz); 59.74 (CCH2O); 67.85 (CH2CH2O); 70.96 (CCHzO); 158.96 (NHCONH); 173.42 (COOH). FAB-MS: 506.19 (MH*). AH6-Azidohexyl).AT-trls[(2-{I(tris{[2-{ferf-butoxycarbonyl)ethoxy]-methyf}methyOamino]carlx>nyl}ethoxy)inethyl]methy1urea (4.1). The HOBt (0.20 g, 1.5 mmol), DIEA (0.30 mL, 1.8 mmol), and EDO (0.33 g, 1.8 mmol) were added to (4) (0.25 g, 0.50 mmol) in 5.0 mL of dry acetonitrBe. Then, the amine (2) (1.14 g, 2.3 mmol) dissolved in 2.5 ml of dry acetonitrite was added, and the reaction mixture was stirred under N2 for 48 h. After removal of the solvent at reduced pressure, the residue was dissolved in MC and washed with 0.5 M Hd and brine. The organic layer was then dried over MgSO*. the solvent was removed in vacuo, and column chromatography (SKD2, 2:1 EtOAc/hexane) yielded a colorless oil (0.67 g, 70%). 1H NMR (CDCIa, 300 MHz): 6 1.45 (s, (CH&C, 81H); 1.36-1.58 (m, CW2CH2CH2CH2, 8H); 2.40-2.47 (m, CHzCHzO gen. 1 & 2, 24H), 3.13 (m, CONHCH2, 2H), 3.26 (t, N3CH2, 6.9 Hz, 2H), 3.62-3.69 (m, CCH2O gen. 1 & 2, CH2CH2O gen. 1 & 2, 48H); 5.36 (t, CH2NHCO, J=6.7 Hz, 1H), 5.68 (br, CONHC, 1H), 6.28 (br, amide NH, 3H). 13C NMR (CDCIa, 75 MHz): 5 26.59, 26.69, 28.91, 30.54 (CH2CH2CH2CH2); 28.22 ((CH8)sC); 36.20 (CH2CH2O gen. 2); 37.43 (CH2CH2O gen. 1); 39.81 (CONHCHz); 51.47 (NaCHz); 58.93 (CCH2O gen. 1); 59.89 (CCH2O gen. 2); 67.15 (CH2CH2O gen. 2); 67.68 (CH2CH2O gen. 1); 69.23 (CCH2O gen. 2); 70.12 (CCH^ gen. 1); 80.57 ((CH3)3C); 158.25 (NHCONH); 171.01 (COOf-Bu) 171.41 (CONH amides). MALDI-MS: 1989.8 (MNa+), 2005.8 (MK*). W-{6-Aminohexyi)-W'-tris[(2-{I{trisa2-(tert-birtoxycarbonyi)ethoxy]-methyt}methyl)arnlno]carbonyl}ethoxy)methyr|methylurea(4.2). Nona-te/f-butyl ester (4.1) (0.37 g, 0.20 rnmol) was stirred with 10 % Pd/C (37.0 mg) in ethanol (20.0 mL) under H2 at room temperature for 12 h. After checking completion of the reaction with TLC, the mixture was filtered with a 0.2 /jm Millipore filter. After the filter paper was rinsed with CH2CI2, the combined solvent was removed in vacuo, and colorless oil was recovered. N-{6-(9-fluorenylmethoxycarbony1)aminohexyl>-W-tris[(2-{[(tris{r2-(tert-butoxycarbonyl)ethoxy]methyl}methyl)amlno]carbonyl}ethoxy)methyl]methylu rea (4.3). The amine (4.2) (0.33 g, 0.17 mmd) and DIEA (33 fJL, 0.19 mmol) were dissolved in 5.0 ml of CHzCfe, and stirred for 30 min under nitrogen atmosphere. 9-Fluorenylmethyi chbroformate (48 mg, 0.19 mmol) in 2.0 ml of CH2CI2was added, and the reaction mixture was stirred for 3 h at room temperature. The solvent was removed under reduced pressure and washed with 0.5 M Hd and brine. The residue was purified with column chromatography (silica, EtOAc) to yield colorless oil (0.18 g, 64%). 1H NMR (CDCIs, 300 MHz): 5 1.45(s, (CH&C, 81 H); 1.23-1.58 (m, CHzCHaCHzC/^z, 8H); 2.37-2.47 (m, CHaCHaO gen. 1 & 2, 24H); 3.10-3.22 (m, CONHCHa, 4H); 3.62- 3.70 (m, CCH2O gen. 1 & 2, CHzCHaO gen. 1 & 2,48H); 4.22 (t, C«(fluorenyl)-CH2> J=7.1 Hz, 1H); 4.36 (d, fluorenyi-CW2, ^=7.1 Hz, 2H); 5.27-5.35 (m, CH2NHCO, 2H); 5.67 (br, CONHC, 1H); 6.25 (br, amide, 3H); 7.28-7.77 (fluorenyl, 8H). 13C NMR (CDCI3, 75 MHz): 6 26.85, 27.02, 30.27, 30.88 (CH2CH2CH2CH2); 28.49 ((CH3)3C); 36.48 (CH2CH2O gen. 2); 37.73 (CHzCHjp gen. 1); 40.03, 41.34 (CONHCH2); 47.68 (CH(fluorenyl)-CH2); 59.22 (CCH2O gen. 1); 60.16 (CCHzO gen. 2); 66.87 (fluorenyK>!2); 67.43 (CH2CHaO gen. 2); 67.98 (CH2CH2O gen. 1); 69.52 (CCH20 gen. 2); 70.42 (CCH2O gen.1); 80.84 ((CHaJaC); 120.28, 125.52, 127.38, 127.98, 141.65, 144.48 (fluorenyl); 156.88 (OCONH); 158.52 (NHCONH); 171.27 (COOf-Bu) 171.65(amide CONH). MALDI-MS : 2186.8 (MNa*), 2002.8 (MK*). W-{6-(9-fluorenyimethoxycarbonyl)amlnohexyl}-A/-trIs[(2-{I(trls{t2-carboxyethoxy]methyl}methyl)amlno]carbonyl}ethoxy)methyrj-methylurea(5). Nona-tert-butyl ester having a protecting group (4.3) (0.12 g, 72 mmol) was stirred in 10 ml of 96 % formic add for 18 h. The formic acid was then removed at reduced pressure at 50 °C to produce colorless oil in a quantitative yield. 1H NMR (CD3COCD3, 300 MHz): 5 1.23-1.51 (m, CH2CW2CH2CH2, 8H); 2.44-2.58 (m, CH^HzO gen. 1 & 2, 24H); 3.15-3.18 (m, CONHCH2, 4H); 3.61-3.75 (m, CCHzO gen. 1 & 2, CHzCHzO gen. 1 & 2, 48H); 4.23 (t, CH(fluorenyl)-CH2, J=7.0 Hz, 1H); 4.35 (d, fluorenyl-CH2, J=7.0 Hz, 2H); 5.85, 6.09 (br, CHzNHCO, 2H); 6.57 (br, CONHC, 1H); 6.88 (br, amide NH, 3H); 7.31-7.88 (fluorenyl, 8H). 13C NMR (CD3COCD3, 75 MHz): 6 27.21, 27.33, 30.69, 30.98 (CH2CH2CH2CH2); 35.31 (C^CHzO gen. 2); 37.83 (CHzCH2O gen. 1); 40.56,41.54 (CONHCH2); 48.10 (CH(fluorenyl)-CH2); 59.93 (CCH2O gen. 1); 61.10 (CCHzO gen. 2); 66.86 (fluorenyl-CH2); 67.81 (CH2CH2O gen. 2); 68.37 (CHaCH gen. 1); 69.80 (COM3 gen. 2); 70.83 (CCHaO gen.1); 120.84, 126.13, 127.98, 128.56, 142.10, 145.16 (fluorenyl); 157.50 (OCONH); 159.82 (NHCONH); 173.20 (amide CONH); 173.93 (COOH). EXAMPLE 3 - Additional Dendron Compounds It is to be noted that while a particular protecting group may be shown with a macromotecute, the compounds are not limited to the specific protecting groups shown. Moreover, white various chains and spacers are depicted indicating an exact molecular structure, modifications are possible according to accepted chemical modification methods to achieve the function of a density controlled, preferably low density, array on a substrate surface. As a point of reference for the short-hand description of the compounds, the left most letter(s) indicates the protecting group; the numeral in brackets indicates the number of branched termini; and the right most chemical entity indicates the chemistry on the branched termini. For example, "A-[27]-acid" indicates anthryimethyl protecting group; 27 termini, and acid groups at the termini. A-[27]-acid (Figure Removed) EXAMPLE 3.1 - Preparation Methods 1.A-[3]-OEt(3) (Figure Removed) Compound 1 reacted with NaC(CO2Et)3 2 in CeHs/DMF at 80°C. 2. A-[3]-OMe (5) (Figure Removed) A-{3]-OEt 3 was reduced with UAIH, or UBHi in ether, reacted with chloroacetic acid in the presence of t-BuOK/t-BUOH, and esterified with MeOH. 3. A-[3]-OTs (7) (Figure Removed) Reduction of A-[3]-OMe 5 with UAIH4 in ether yields triol compound 6, which is tosylated to compound 7. 4.A-[9]-OEt(8) (Figure Removed) A-[3]-OTs 7 was treated with NaC(CO2Et)3 in C6Ho)propyfJ-3-^ hydrochtoride (EDC) and 1-hydroxybenzotriazote hydrate (HOBT). 3.A-{3]-tribromide(6) (Figure Removed) (d)The alcohol was used to synthesize tribromide by bromination with HBr/H2SO4at100°C. 4. [1]-CN-[3]-OBzl (8) (Figure Removed) (e) The triol 1 was treated with benzyl chloride to give trisether using Me2SO and KOH. (f) The trisether 8 was cyanoethylated affording the nitrile compound 9. Acrylonitrile, nBu3SnH, and azobisisobutyronitrile was added in PhCH3 including compound 8 at 110°C. 5. [1]-OH-[3]-OBzl (11) (Figure Removed) (g) The nitirle compound 9 was hydrolyzed to give compound 10 with carboxylic acid cleanly in such condition as KOH, EtOH/H2O, HjjOa, A. (h) The compound 10 with a carboxylic acid was proceeded with excess 1.0 M BH3THF solution to converse the acid into alcohol. 6. [1]-Alkyne-[3]-OBzl (13) (Figure Removed) (i) The alcohol was transformed Into chloride (CH2CI2) with excess SOCI2 and a catalytic amount of pyridine. Q) The chloride was reacted with lithium acetylide ethylenediamine complex in dimethylsulphoxide at 40°C. 7. A-[3]-Alkyne-[9]-OBzl (14) (Figure Removed) (k) The A-[3]-OBzl 6 was alkylated with 4 equivalents of terminal alkyne building block 13, hexamethylphosphoric rtriamide (HMPA), lithium diisopropylamide (IDA), and tetramethylethylenediamine (TMED) at 0-40°C for 1.5 h. EXAMPLE 3.7(Figure Removed) A-[3]-Alkyne-[9]-OBzl 14 was reduced and deprotected with Pd-C/H to produce A-[9]-OH 15 in EtOH and THF solution including 10% Pd-C/H at 60°C for 4d. (Figure Removed) The alcohol was smoothly converted into the nonabromide employing SOBr2 in CH2CI2 at 40°C for 12 h. And then the nonabromide compound was alkylated with 12 equivalents of [1]-Alkyne-[3]-OBzl 13 to give 49% of A-[9]-Alkyne-[27]- OBzl 16. A-[9]-Alkyne-[27J- OBzl 16 were reduced and deprotected in one step with Pd-C/H in EtOH and THF solution including 10% Pd-C/H at 60"C for 4d yielding 89% of A-[27]-OH. A-[27]-OH was oxidized by RuO4 treating with NH4OH or (CH3)4NOH to achieve 85% of A-[27]-COOH 17. EXAMPLE 3.8 1)[G1]-(OMe)2(3) (Figure Removed) A mixture of compound 1 (1.05 mol equiv.), 3,5-dimethoxyben2yl bromide (1.00 mol equiv. 2), potassium carbonate (1.1 mol equiv.) and 18-C-6 (0.2 mol equiv.) in dry acetone was heated at reflux under nitrogen for 48h. The mixture was cooled and evaporated to dryness, and the residue was partitioned between OfeClz and water. The aqueous layer was extracted with CH^b (3 x), and the combined organic layers were dried and evaporated to dryness. The crude product was purified by flash chromatography with EtOAc-CH^ as eluent to give compound 3. 2)[G1HOHM4) (Figure Removed) Methyl ether group of compound 3 was deprotected by BBr3 in EtOAc solution for 1 h, and the crude product was purified by flash chromatography with MeOH-EtOAc as eluent to give compound 4. 3)[G2]-(OMe)4(5) (Figure Removed) A mixture of [G1]-(OH)2 (1.00 mol equiv. 4), 3,5-dimethoxybenzyl bromide (2.00 mol equiv. 2), potassium carbonate (2.1 mol equiv.} and 18-C-6 (0.2 mol equiv.) in dry acetone was heated at reflux under nitrogen for 48h. The mixture was cooled and evaporated to dryness, and the residue was partitioned between CH2CI2 and water. The aqueous layer was extracted with CH2CI2 (3 x), and the combined organic layers were dried and evaporated to dryness. The crude product was purified by flash chromatography with EtOAc-CH2CI2 as eluent to give compound 5. 4)[G2]-(OH)4(6) (Figure Removed) Methyl ether group of compound 5 was deprotected by BBr3 in EtOAc solution for 1 h, and the crude product was purified by flash chromatography with MeOH-EtOAc as eluent to give compound 4. 5) [G3MOMe)B (7) (Figure Removed) A mixture of [G2]-(OH)4 (1.00 mol equiv. 6), 3,5-dimethoxybenzyl bromide (4.00 mol equiv. 2), potassium carbonate (4.1 mol equiv.) and 18-C-6 (0.2 mol equiv.) in dry acetone was heated at reflux under nitrogen for 48h. The mixture was cooled and evaporated to dryness, and the residue was partitioned between CHjCfe and water. The aqueous layer was extracted with ChfeC^ (3 x), and the combined organk: layers were dried and evaporated to dryness. The crude product was purified by flash chromatography with EtOAc-CH^a as eluent to give compound 7. 6) [G3MOH), (8) (Figure Removed) Methyl ether group of compound 7 was deprotected by BBr3 in EtOAc solution for 1 h, and the crude product was purified by flash chromatography with MeOH-EtOAc as eluent to give compound 8. EXAMPLE 4 - Assembly of the Dendron on a Substrate TMAC (N-trimethoxysilylpropyl-N,N,N-trJmethylammonium chloride) was self-assembled on oxide glass instead of APDES. The dendrimer layer on TMAC layer did not need to cap the residual amine. Aminosllylation with TMAC. Clean substrates (slide glass) were placed into a solution of TMAC (2ml_) and acetone (100mL) for 5 h. After the self-assembly, the substrates were taken out of the flask, washed with acetone. The substrates were placed in an oven, and heated at 110 °C for 40 min. After immersion in acetone, the substrates were sonicated for 3 min. The washed substrate was placed in a Teflon vessel, and placed in a glass container with a big screw cap lined with an O-ring, and eventually the container was evacuated (30-40 mTorr) to dry the substrate. (Figure Removed) Structure of TMAC (N-trimethoxysilylpropyl-N,N,N-trimethylammonium chloride). Self-assembly of the Fmoc-spacer-[9]acid was performed in same condition to the case of CBz-[9]acid with exception of capping of the residual amines by acetic anhydride Self-Assembly of the Fmoc-spacer-[9]acld (5). A certain amount of the Fmoc-spacer-[9]acid (5) was dissolved iq a mixed solvent (DMF:deionized water = 1:1 (v/v)) to make a solution of 20 ml. The solution was added into a Teflon vessel, and subsequently pieces of the above prepared aminosilylated slide glass were placed in the solution. While allowing the flask at room temperature to self- assemble, each piece of the substrate was taken out of the solution after 1 day. Right after being taken out, the plate was washed with a copious amount of deionized water. Each substrate was sonicated for 3 min in deionized water, a mixture of deionized water-methanol (1:1 (v/v)), and methanol in a sequential manner. After sonication, the substrates were placed in a Teflon vessel, and placed in a glass container with a big screw cap lined with an O-ring, and eventually the container was evacuated (30-40 mTorr) to dry the substrate. Deprotection of Fmoc from the Self-Assembled Fmoc-spacer-[9]acid (5). Teflon vessels containing 5 % piperidine in DMF were prepared. The self-assembled substrates were immersed in the vessels, and stirred for 20 min. Each substrate was sonicated for 3 min in acetone, and MeOH in a sequential manner and evacuated in a vacuum chamber (30-40 mTorr). EXAMPLE 5 - p53 Microarray on Dendron (9-acid and 27-acid) Modified Surface Seven codons, 175, 215, 216, 239. 248, 273. and 282 which are already known to be missense mutational hotspots with unusually high frequency were selected for this study. Codons 175,248,273, and 282 of 7 codons were taken from the, international TP53 mutation database (IARC, http//:www-p53.iarc.fr/p53DataBase.htm) and the other three codons 215, 216, and 239 from Korean p53 mutational hotspot database. The capture probe sequences (the DMA immobilized on dendron-modffied surface) for seven codons were designed by software and their lengths were 15-23 mer varied from codon to codon to set Tm to around 55 °C. EXAMPLE 5.1 - Detection of 7 hot spot mutations of p53 gene using single dendron-modifled surface The dendron-modifled substrates were applied to the detection of single mutation of p53 tumor suppressor gene in cancer cell line. Target DNA samples (100-200 mer) which span 7 hot spot codons (175, 215, 216, 239, 248, 273, and 282) were amplified from the DNA extracted from cancer cells by random priming (See EXAMPLE 5.8) and allowed to hybridize with the capture probe (oligonucleotides of 15-25 mer) corresponding to the 7 hot spot codons that had been immobilized. The fluorescence intensity of each hybridized spot was determined with confocal laser scanner and the SNP discrimination efficiency was calculated. This study shows the quality of DNA microarray on dendron-modified surface for the detection of single mutation in real target sample. EXAMPLE 5.2 - Effect of length of probe olfgonucleotfde with T30 on hybridization efficiency and SNP discrimination The effect of the length of capture probe for the SNP discrimination efficiency was tested by varying the length of capture probes with T30. After immobilizing capture oligonucleotides corresponding to codons 175 and 239 containing T30 by linking the 5' end of the specific sequence and the terminal primary amino group on dendron-modified surface, p53 target DNA was hybridized and fluorescence intensity was measured. This study shows dependence of the SNP discrimination efficiency and signal intensity on the length of the capture probe. EXAMPLE 5.3 - Concentration of capture probe vs. intensity; and Concentration of capture probe vs. SNP discrimination Dependence of signal intensity and SNP discrimination efficiency on the concentration of capture probes was investigated. Capture probes on dendron-modified surface, at various concentrations, were allowed to hybridize with target DNA and the fluorescence intensity and SNP discrimination efficiency were determined. Optimal concentration of capture probe for p53 was determined. EXAMPLE 5.4 - Concentration of target probe vs. Intensity; and Concentration of target probe vs. SNP discrimination Dependence of signal intensity and SNP discrimination efficiency on the concentration of target probes was investigated. Target DMAs of various concentration were applied to hybridization and the fluorescence intensity and SNP discrimination efficiency were determined. This work provides the dynamic range of DNA microarray on dendron-modified surface. EXAMPLE 5.5 - Detection of mutation in mixed target samples Point mutations with target samples in which the mutated target sequences exist in a small portion compared with normal sequence (5 or 10%) may be detected. Samples containing two kinds of target DNAs were prepared with different molar ratio and used for hybridization to detect single point mutation in certain codon in mixtures of normal as well as mutated target DNA. This work has clinical importance for detecting early stage cancer. EXAMPLE 5.6 - Detection of mutation in ten unknown colon cancer cell lines The inventive system is used to detect mutations in unknown cancer cell lines. EXAMPLE 5.6.1 - Cell cultures and genomic DNA extraction. The colon cancer cell lines SNU-C1, SNU-C5, COLO 201, COLO 205, DLD-1, LS 513, HCT-15, LS 174T, HCT 116, and SW480 were purchased from KCLB (Korea Cell Line Bank, Seoul, Korea). Cells were cultured in RPMI 1640 supplemented with 10% fetal bovine serum (FBS), 100 ug/ml streptomycin and 100 U penicillin (GibcoBRL, Carlsbad, CA) and incubated in 5% CO2 at 37 °C. The colon cancer cells (2x106 cells) were harvested for genomic DNA extraction by Invisorb® spin cell mini kit (Invitek, Berlin, Germany) following the manufacturer's instructions. From these genomic DNAs, p53 target DNAs were prepared (see EXAMPLE 5.8.2) and DNA microarray experiment were performed using the same procedure described above. EXAMPLE 5.7 - Effect of length of target probe on hybridization efficiency and SNP discrimination By preparing different lengths of target DNAs by several different methods such as random priming, PCR, and DNase degradation the effect of length of target probe on hybridization and SNP discrimination efficiency was investigated. EXAMPLE 5.8 -Experimental Protocol EXAMPLE 5.8.1 - Genomic DNA samples Genomic DNAs of SNU-ceN Br.es (SNU-61, 216, 475, 563, 601, 668, 761, and 1040) were kind gifts from Jae-Gab Park, College of Medicine in Seoul National University. The provided SNU-cell lines were human carcinoma cell lines from individual Korean patients. The characteristics of these cell lines were previously described and have been used in various studies (Bae IS et al., 2000, Park JG et at., 1997, Kang MS et al., 1996, Yuan Y et al., 1997, 378-87). EXAMPLE 5.8.2 - Subclonlng and sequencing p53 genes, especially between exon 5 and exon 8, for each cell lines were amplified by PCR with 2 pairs of synthetic oligonucleotide primers used in the previous report: Exon 5 Fwd I, 5'- CTG ACT TTC AAC TCT GTC TCC T - 3' (SEQ ID NO:5); Exon 5 Fwd II, 5'- TAG TCC CCT GCC CTC AAC AA - 3' (SEQ ID N0:6); Exon 8 Rev I, 5'- TGC ACC CTT GGT CTC CTC CAC - 3' (SEQ ID NO:7); Exon 8 Rev II, 5'- CTC GCT TAG TGC TCC CGG G - 3' (SEQ ID NO:8) (Kang MS et al., 1996). Each genomic DNA was amplified with 10 pmoles of first primer pair (exon 5 Fwd I and Exon 8 Rev I, corresponding to intron 4 and intron 8), 250 uM dNTP mix, 2.5U Taq polymerase (NEB) in 1x TherrnoPol buffer (supplemented with Taq polymerase) for 20 pi of total reaction volume in Multiblock System (Hybaid, UK) using the following settings: initiation activation of the polymerase at 95°C for 1 minute, then 20 cycles of 95°C for 30 sec, 58°C for 30 sec, 72°C for 90 sec, followed by final elongation step at 72°C for 5 min. First PCR products were diluted and used as template for second PCR. The amplified genomic DNA PCR products were diluted 20 fold and used for the second nested PCR under the same conditions as the previous step except PCR was performed with 10 pmoles of the second primer pair (exon 5 Fwd ll and exon 8 Rev II, corresponding to exon 5 and exon 8) and the cycle for amplification was increased to 25 cycles. The final nested PCR products were purified by gel extraction method. PCR products from genomic DNA were ligated into pGEM T-easy vector (Promega) and transformed to DH5a cells. Subcloned plasmid was purified by QIAGEN Plasmid Min kit (QIAGEN Inc., Valencia, CA) for sequencing analysis. Bidirectional sequencing was performed using pUC/M13 Forward and Reverse Sequencing Primer as follows: M13 FWD 5'-GTT TTC CCA GTC ACG ACG TTG -3' (SEQ ID NO:9) and M13 REV 5' - TGA GCG GAT AAC AAT TTC ACA CAG -3' (SEQ ID NO:10). EXAMPLE 5.8.3 - Preparation of target probe DNA target probes spanning SNP sites were random primed and labeled in a Multiblock System (Hybaid, UK) using 50 ng of template DNA with 50 U Klenow enzyme (NEB), 1x EcoPol buffer supplemented with Klenow enzyme, 6|jg of random octamer (synthesized by Bionics), low dT dNTP mix (100uM dA,G,CTP / 50uM dTTP) and 50uM Cyanlne3-dUTP (NEN) in 20 Ml of total reaction volume at 37°C for 2 hours. Unincorporated nudeotides were separated by QIAGEN MinElute PCR purification kit (QIAGEN Inc., Valencia, CA). After quantitative and qualitative (specific activity, number of nucleotide per an incorporated fluorescent dye) analysis using UVA/is spectrophotometer, qualified products were applied to the hybridization. EXAMPLE 5.8.4 - Cell cultures and genomic DNA extraction. The colon cancer cell lines SNU-C1, SNU-C5, COLO 201, COLO 205, DLD-1, LS 513, HCT-15, LS 174T, HCT 116, and SW480 were purchased from KCLB (Korea Cell Une Bank, Seoul, Korea). Cells were cultured in RPMI 1640 supplemented with 10% fetal bovine serum (FBS), 100 \ig/m\ streptomycin and 100 U penicillin (GibcoBRL, Carlsbad, CA) and incubated in 5% CO2 at 37 ti. The colon cancer cells (2x106 cells) were harvested for genomic DNA extraction by Invisorb* spin cell mini kit (Invitek, Berlin, Germany) following the manufacturer's Instructions. EXAMPLE 6 - Fixing Protein Probe on the Dendron EXAMPLE 6.1 - Arraying NHS-biotin to the dendrimer modified slide glass. Produce the spotting solution of succinimidyl D-biotin (1.0mg) in 1mL sodium bicarbonate buffer 50 mM and DMSO (40 % v/v). Arraying NHS-biotin to the dendrimer modified slide glass was performed using Microsys 5100 microarrayer (Cartesian Technologies, Inc, USA) in a class 10,000 clean room. After arraying and incubating for 1 h in a humidified chamber (~ 75 % humidity), the biotin microarrays were subsequently washed for 2 h each with DMF (50°C) THF and aqueous wash with MBST (50 mM MES, 100 mM NaCI, 0.1% Tween- 20, pH 6.0). Slides were rinsed with double-distilled water, dried, and either used immediately or stored at room temperature for several days. EXAMPLE 6.2 - Detection of proteln/llgand interactions. This method according to Hergenrother, P. J.; Depew, K. M.; Schreiber, S. L. J. Am. Chem. Soc. 2000, 122, 7849 was followed. Before adding Cy3-labeted streptavidin solution, the slides were blocked for 1 h with MBST supplemented with 3% bovine serum albumin (BSA). After a brief rinse, the sides were exposed to Cy3-tebeted streptavidin solution for 30 min at room temperature. This solution was prepared by diluting stock solutions of the appropriate proteln(s) with MBST supplemented with 1% BSA at a concentration of 1ug/mL After incubation, the slides were rinsed once with MBST and then gently agitated with four changes of MBST over the course of 12 min. The slides was dried and scanned using a commercial confocal laser scanner, ScanArray* Lite (GSI Lumonics). Quantitative microarray analysis software, ImaGene (BioDiscovery, Inc.) was used for image acquisition and fluorescence intensity analysis. EXAMPLE 7 - Methods For Making Controlled Pore Glass Bead That Includes Size-Controlled Macromolecule Aminopropyl group tethered controlled pore glass beads (AMPCPG; 80-120 mesh; mean pore diameter, 50 nm or 300 nm) and controlled pore glass beads modified with a long chain aminoalkyl group (LCAA-CPG; 80-120 mesh; mean pore diameter, 50 nm) were purchased from CPG, Inc. 1,4-Butanediol diglycidyl ether, 1,3-diaminopropane, reduced glutathione (GSH), N-(3-methylaminopropyl)-N'-ethylcarbodiimide (EDO), N-hydroxysuccinimide (NHS), N-(9-fluorenylmethoxycarbonyloxy)chloride (Fmoc-CI), piperidine, 4-maleimidobutyric acid N-hydroxysuccinimide ester (GMBS), phosphate buffered saline tablets (PBS) were obtained from Sigma-Aldrich. All other chemicals were of analytical reagent grade and were used without further purification. Deionized water (18 MQ-cm) was obtained by passing distilled water through a Bamstead E-pure 3-Module system. UV-vis spectra were recorded on a Hewlett-Packard diode-array 8453 spectrophotometer. EXAMPLE 7.1 - Immobilization of Glutathione on the Dendron-modffied CP6 (Sample E1 and E3). (i) Modification with Fmoc-(3)acid : AMPCPG (dry weight 0.70 g) was washed thoroughly with acetone with a glass filter. After drying in vacuum, a mixture of 1,4-butanediyl diglycidyl ether (1.0 ml_) and carbonate buffer solution (2.0 ml, pH=11) was added to AMPCPG (surface capacity: 91.8 A/mol/g, surface area: 47.9 m2/g). After shaking for 24 h at room temperature, the resulting beads were separated from the solution by filtration and washed thoroughly with deionized water and subsequently with acetone. Then a vial containing this sample was shaken with a mixture of 1,3-diaminopropane (1.0 ml) and carbonate buffer solution (pH=11) for 24 h at room temperature. After washing thoroughly, a mixture of 2-mercaptoethanol (1.0 ml) and aqueous sodium bicarbonate solution (2.0 mL, pH=8.5) was employed for blocking the residual epoxy group on the surface. Subsequently, an aqueous solution of dimethylformamide (30 % DMF (v/v)) dissolving Fmoc-(3)acid (14 mg, 21.3 //mol), N-(3-methylaminopropylJ-N'-ethylcarbodiimide (15 mg, 77 //mol) and N-hydroxysuccinimide (9.0 mg, 77 ;/mol) was introduced into a vial containing the beads. After shaking for 11 h at room temperature, the beads were washed thoroughly with deionized water and subsequently with acetone, (ii) Blocking step: Acetic anhydride (1.0 mL) in anhydrous methylene chloride (2.0 ml) was allowed to react with the residual amine overnight at room temperature. (Hi) Deprotection step: After washing the beads with methylene chloride and subsequently with acetone, 20 % piperidine in DMF (3.0 ml) was added in a vial holding the beads, and the vial was shaken for 30 min. (iv) LJgand-immobilization step: A mixture of 1,4-butanediyl diglycidyl ether (1.0 mL) and carbonate buffer solution (2.0 mL, pH=11) was added again into the vial, and the mixture was shaken for another 24 h at room temperature. After washing the beads with deionized water and subsequently with acetone, the reduced glutathione (GSH, 5.4 mg, 17.6 //mol) in sodium bicarbonate solution (3.0 mL, pH 8.5) was added into a vial containing the beads, and the vial was shaken for 12 h at room temperature. After washing the beads, a mixture of 2-mercaptoethanol (1.0 mL) and aqueous sodium bicarbonate solution (2.0 ml, pH=8.5) was added into the vial containing the beads. Finally, the beads were separated, washed, dried in vacuum, and stored at 4 °C under dry nitrogen atmosphere. The same steps were followed exactly to prepare the sample E3 as described above, except that Fmoc-(9) acid was used instead of Fmoc-(3) acid. EXAMPLE 7.2 - Preparation of Other GSH tethered Matrices for Control Experiment (Sample CS, CL, and A): (i) Sample CS and CL: GSH was immobilized directly on both AMPCPG and LCAA-CPG through GMBS linker. The beads (0.10 g) were washed thoroughly with acetone with a glass filter. After being dried in vacuum, a mixture of DMF and sodium bicarbonate buffer (1.0 ml, 3:7 (v/v), pH=8.5) dissolving 4-maleimidobutyric acid N-hydroxysuccinimide ester (GMBS, 3.0 mg, 11 i/mol) was added into a vial containing the beads. After four hours of shaking at room temperature, the resulting beads were separated from the solution by filtration and washed thoroughly with detonized water and subsequently with acetone. Finally, acetic anhydride (1.0 mL) in anhydrous methylene chloride (2.0 mL) was allowed to react with residual amine group on the matrix. After thorough washing, glutathione (GSH, 3.4 mg, 11 //mol) in PBS buffer (1.0 mL) was added into a vial containing the beads, and the vial was shaken for 12 h at room temperature. After 2-mercaptoethanol (1.0 mL) was used to block the residual maleimido group, the beads were separated, washed, dried in vacuum, (ii) Sample A: The same modification steps for E1 and E3 were followed to modify AMPCPG with 1,4-butanediyl diglycidyl ether and 1,3-diaminopropane. After the capping with 2-mercaptoethanol, 1,4-butanediyl diglycidyl ether was employed to generate an epoxy group. Finally, glutathione was immobilized, and 2-mercaptoethanol was used to open the remaining epoxy group on the beads. EXAMPLE 7.3 - Determination of Amine Density on the Modified Beads: Either modified beads on the way to E1 or E3 or beads for control experiments (10 mg) were taken into an e-tube. In parallel, 9-fluorenylmethyl chloroformate (Fmoc-CI, 1.75 mg) and Na2CO3 (1.45 mg) were placed into a separate glass vial, and a mixed solvent (2:1 (v/v) 1,4-dioxane and water, 2.5 mL) was added to dissolve the reagents. One fifth of the solution was taken and transferred into the e-tube containing the beads. The tube was placed into a vial, and the vial was shaken for 12 h at room temperature. The beads were separated with a glass filter, and the porous materials were washed with deionized water and subsequently with acetone. After being dried in vacuum, 20 % piperidine in DMF (0.50 ml) was added into an e-tube containing the beads. The beads were allowed to react with piperidine for 30 min. Then the resulting solution from the tube was transferred carefully into a new e-tube, and the beads were washed with 20 % piperidine in DMF (0.25 ml) twice. All of the solution was added into the prevbus e-tube. Then the solution was mixed with a certain volume of methanol to adjust the absorbance. The absorbance at 301 nm was measured using a UV/Vis spectrometer, and a relevant solvent was used for the background correction. To increase reliability, the measurements were carried out with five different samples. For calibration, we prepared a series of the solution of N-Fmoc- ethanolamine (or 9-fluorenylmethyl N-(2-hydroxyethyl)carbamate) (30 M - 70 M) in 20 % piperidine in DMF. After allowing 30 min for the reaction, the solutions containing dibenzofulvene were utilized for measuring absorbance, and calculating the absorption coefficient. EXAMPLE 7.4 - Preparation of GST Fusion Protein Lysate: „ GST-fusion proteins were prepared as described before, Kim, J. H.; Lee, S.; Kim, J. H.; Lee, T. G.; Hirata, M.; Sun, P.-G.; Ryu, S. H.; Biochemistry 2002, 41, 3414-3421, which is incorporated by reference herein in its entirety. For large scale cultures, the single colony containing a recombinant pGEX plasmid was incubated into 200 ml of 2X YTA medium. After growing to log phase, gene expression was induced with IPTG for another 6 h. Subsequently, cells were pelleted by centrifugatfon and washed with 1X PBS. Then £. coli was lysed in 10 mL hypotonic buffer (20 mM Tris, 150 mM NaCI, 1.0 mM MgCI2, 1.0 mM EGTA, pH 7.4) containing 0.50 mM PMSF by the sonicator. The proteins were obtained by the removal of insoluble material. EXAMPLE 7.5 - Binding assays: (i) The effect of chain length: The prepared beads CL (5.72 mg), CS (6.97 mg), E1 (10.0 mg), and E3 (14.8 mg) were incubated separately with the mixed solution including GST lysates in 0.8 mL of the incubation buffer (20 mM Tris, 150 mM NaCI, 1.0 mM MgCI2, 1.0 mM EGTA, 1 % TX-100, 0.10 mM PMSF, pH 7.4, 0.50 mM PMSF) for 1 h at 4°C, washed with the 10 bed volume of incubation buffer for three times and then 100 pL of the SDS-sample buffer was added. After the tubes were cooked for 5 min at 95°C, 20 yuL samples were utilized for SDS-PAGE and the gel was stained by CBB G-250 staining solution, (ii) Selectivity of the dendron-treated matrices: 10 mg of samples A, E1, and E3, as well as 100 A/g of purified GST or GST-fused protein lysate were used in this experiment. The other steps were same as described above. EXAMPLE 7.6 - Elution of GST Fusion Proteins from Glutathione Sepharose-4B, E1 and E3: Glutathione Sepharose-4B, E1, and E3 were processed as described in 'Binding assays (i)'. The amount of the protein bound to beads was determined using Image gauge V3.12 (FUJI PHOTO FILM CO., LTD.). The same steps were followed for PX domain of