COMPOSITION FOR DETECTING OR MEASURING ANALYTES

Abstract

The present disclosure relates to a composition for detecting or measuring an analyte and an analysis method using the composition. In particular, efficiency and performance of sample analysis may be greatly improved through the composition and analysis method of the present disclosure.

Claims

1. A composition containing a complex compound represented by Formula 1:
[M].sub.n-L.sub.1-N.sub.1  [Formula 1] wherein n is an integer ranging from 2 to 100; M is a repeatable unit compound; L.sub.1 is either a direct bond between M and N.sub.1 or a linker; and N.sub.1 is a first binding moiety that binds to the analyte.

2. The composition of claim 1, wherein adjacent M and M are linked together by a pH-specifically or catalyst-specifically cleavable bond to form a polymer.

3. The composition of claim 1, wherein M has a mass-to-charge ratio (m/z) of 30 to 3,000.

4. The composition of claim 1, wherein M is represented by Formula 2:
(X.sub.1X.sub.2 . . . X.sub.m)  [Formula 2] wherein m is an integer ranging from 1 to 100; and X.sub.1 to X.sub.m are each independently an amino acid, amino acid analog, peptide, peptide analog, monosaccharide or oligosaccharide unit.

5. The composition of claim 4, wherein X.sub.1 or X.sub.m is isoleucine, lysine, serine, arginine or threonine.

6. The composition of claim 1, wherein the first binding moiety comprises at least one selected from the group consisting of a probe, an antisense nucleotide, an antibody, an oligopeptide, a ligand, PNA (peptide nucleic acid) and an aptamer, which bind to the analyte.

7. The composition of claim 1, wherein the first binding moiety comprises at least one selected from the group consisting of Chemical Formulas 1 to 5: ##STR00006## wherein p is an integer ranging from 7 to 20, and * is a portion linked to [M].sub.n or L.sub.1.

8. The composition of claim 1, wherein the linker comprises at least one selected from among Chemical Formulas 6 to 8:
* —C.sub.qH.sub.2q—*  [Chemical Formula 6]
*—C.sub.qH.sub.2qCOO—*  [Chemical Formula 7]
*—H.sub.2NCOC.sub.qH.sub.2qS—*  [Chemical Formula 8] wherein q is an integer ranging from 1 to 5; and * is a linking portion.

9. The composition of claim 1, containing two or more different complex compounds represented by Formula 1.

10. A kit for analyte detection comprising the composition of claim 1.

11. A method for analyzing an analyte, the method comprising: reacting the analyte with the composition of claim 1; and detecting or measuring M in the complex compound contained in the composition.

12. The method of claim 11, wherein the analyte is present in a biological sample isolated from a subject of interest.

13. The method of claim 12, further comprising an immobilization step of immobilizing the analyte by bringing the analyte into contact with a second binding moiety.

14. The method of claim 13, wherein the second binding moiety comprises at least one selected from consisting of a probe, an antisense nucleotide, an antibody, an oligopeptide, a ligand, PNA (peptide nucleic acid) and an aptamer, which bind specifically to the analyte.

15. The method of claim 13, wherein the second binding moiety is bound to an immobilization support, a carrier or biotin to form a second binding moiety-immobilization support conjugate or second binding moiety-carrier conjugate.

16. The method of claim 11, further comprising a cleavage step of cleaving [M]n in the complex compound into units M, after the reaction step.

17. The method of claim 16, wherein the cleavage into the units M in the cleavage step is performed by an enzyme or a synthetic catalyst.

18. The method of claim 16, wherein [M]n in the complex compound is cleaved into n units M in the cleavage step, so that detection or measurement sensitivity of M increases.

19. The method of claim 11, further comprising treating with a metal salt in the reacting step.

20. The method of claim 11, wherein the composition contains two or more different complex compounds represented by Formula 1, thus enabling simultaneous analysis of multiple analytes, samples derived from multiple subjects, or multiple samples derived from a subject.

Description

BRIEF DESCRIPTION OF DRAWINGS

[0143] FIGS. 1 to 3 are schematic views showing methods for analyzing an analyte according to examples of the present disclosure.

[0144] FIG. 4 shows a process for producing a detection sensor according to an embodiment of the present disclosure in Preparation Example 1.

[0145] FIG. 5 shows the results of confirming coupling by the Kaiser test according to an embodiment of the present disclosure in Preparation Example 1.

[0146] FIG. 6 shows a process for producing a detection sensor according to an embodiment of the present disclosure in Preparation Example 2.

[0147] FIG. 7 shows a process for producing a detection sensor according to an embodiment of the present disclosure in Preparation Example 3.

[0148] FIG. 8 shows an aptamer-MNP conjugate according to an embodiment of the present disclosure, produced in Preparation Example 4.

[0149] FIG. 9 shows a process for producing an aptamer-MNP conjugate according to an embodiment of the present disclosure in Preparation Example 4.

[0150] FIGS. 10a, 10b, 11a and 11b show the results of mass spectrometry of peptide units according to an embodiment of the present disclosure, produced in Preparation Example 6.

[0151] FIG. 12 shows units according to an embodiment of the present disclosure, synthesized in Preparation Example 7.

[0152] FIG. 13 shows M according to an embodiment of the present disclosure, synthesized in Preparation Example 7.

[0153] FIG. 14 shows M according to an embodiment of the present disclosure and units cleaved therefrom, obtained in Preparation Example 8.

[0154] FIG. 15 shows the results of mass spectrometry of peptides according to an embodiment of the present disclosure, produced in Experimental Example 1.

[0155] FIG. 16 shows the results of confirming the amplification effect of peptides according to an embodiment of the present disclosure in Experimental Example 2.

[0156] FIG. 17 shows the results of confirming the amplification effect of peptides according to an embodiment of the present disclosure in Experimental Example 2.

[0157] FIG. 18 shows the results of confirming the amplification effect of peptides according to an embodiment of the present disclosure on improvement in the sensitivity of detection during mass spectrometry in Experimental Example 2.

[0158] FIG. 19 shows the results of confirming the amplification effect of peptides according to an embodiment of the present disclosure on improvement in the sensitivity of detection during mass spectrometry in Experimental Example 3.

[0159] FIG. 20 shows a quantification method according to an embodiment of the present disclosure in Experimental Example 4.

[0160] FIG. 21 shows a magnetic field treatment method according to an embodiment of the present disclosure in Experimental Example 4.

[0161] FIG. 22 shows an [M].sub.n-L.sub.1-N.sub.1-analyte-second binding moiety-carrier conjugate according to an embodiment of the present disclosure in Experimental Example 4.

[0162] FIG. 23 shows the results of quantifying the expression levels of proteins 1 to 4 according to an embodiment of the present disclosure in Experimental Example 5.

[0163] FIG. 24 shows the structure of a complex compound according to an embodiment of the present disclosure, produced in Experimental Example 6.

[0164] FIG. 25 shows a method for mass spectrometry after cleavage into SLVPR fragments in a complex compound according to an embodiment of the present disclosure in Experimental Example 6.

[0165] FIG. 26 shows a method for fluorescence analysis using a complex compound according to an embodiment of the present disclosure in Experimental Example 6.

[0166] FIG. 27 graphically shows the change in sensitivity as a function of the concentration of an analyte in mass spectrometry performed using a complex compound according to an embodiment of the present disclosure in Experimental Example 6.

[0167] FIG. 28 graphically shows the change in sensitivity as a function of the concentration of an analyte in fluorescence analysis performed using a complex compound according to an embodiment of the present disclosure in Experimental Example 6.

MODE FOR INVENTION

[0168] Hereinafter, the present disclosure will be described in detail with reference to examples. However, the following examples merely illustrate the present disclosure, and the scope of the present disclosure is not limited by the following examples.

EXAMPLES

[0169] The meanings of the abbreviations used in the following Examples of the present disclosure are shown in Table 1 below.

TABLE-US-00001 TABLE 1 Abbreviation Meaning A.A Amino acid ACN Acetonitrile AC2O Acetic anhydride Boc Tert-butyloxycarbonyl Wang resins Wang resins CuCl.sub.2 Copper chloride DIC N,N′-diisopropylcarbodiimide DMAP Dimethylaminopyridine DMF N,N′-dimethylformamide DIPEA Diisopropylethylamine HOBt N-hydroxybenzotriazole HNA 9-9-hydroxynonanoic acid Fmoc 9-fluorenylmethoxy carbonyl MeOH Methanol TFA Trifluoroacetic acid PEG Polyethylene glycol

[Preparation Example 1] Production of Detection Sensor of Chemical Formula 9

[0170] FIG. 4 shows a process of synthesizing a polymer (surrogate peptide), which is used to synthesize the complex compound represented by the following Chemical Formula 9 according to the present disclosure, and a process of linking the complex compound to a first binding moiety.

##STR00003##

[0171] As shown in FIG. 4, for solid phase peptide synthesis, using Wang resin and EDCI synthesis, Fmoc-A.A-OH, HOBt and DIC were dissolved in DMF, and the solution was added to a reaction vessel and stirred. Capping of the unreacted sites of the resin was performed using AC2O. Deprotection of Fmoc was performed with piperidine. Similarly, Fmoc-A.A-OH, HOBt and DIC were dissolved in DMF, and the reaction solution was added to the reaction vessel and then stirred. Thereafter, the completion of coupling was monitored through the Kaiser test as shown in FIG. 5. Coupling of the rest of the amino acids in the sequence was performed using DIC/HOBt. Peptidyl resin was dried and taken for total cleavage. Peptidyl resin was treated with TFA at room temperature. After filtration, a solid was isolated from the filtrate using MTBE.

[Preparation Example 2] Production of Detection Sensor of Chemical Formula

[0172] FIG. 6 shows a process for synthesizing a detection sensor complex compound represented by the following Chemical Formula 10 according to the present disclosure.

##STR00004##

[0173] As shown in FIG. 6, chloroacetic acid was added to the * site of Chemical Formula 2, and then a peptide polymer was linked thereto as shown in Chemical Formula 10 above.

[Preparation Example 3] Production of Detection Sensor of Chemical Formula 11

[0174] FIG. 7 shows a process for synthesizing a detection sensor complex compound represented by the following Chemical Formula 11 according to the present disclosure.

##STR00005##

[0175] As shown in FIG. 7, for solid phase peptide synthesis, Wang resin was placed in a solid phase peptide synthesis vessel. HNA was dissolved in DMF, and using EDCI synthesis, HOBt and DIC were dissolved in DMF and added to the reaction vessel, followed by stirring. Capping of the unreacted sites of the resin was performed using AC2O. Deprotection of Fmoc was performed with piperidine. Similarly, Fmoc-A.A-OH, HOBt and DIC were dissolved in DMF, and the reaction solution was added to the reaction vessel and then stirred. Coupling of the rest of the amino acids in the sequence was performed using DIC/HOBt. Peptidyl resin was dried and taken for total cleavage. Peptidyl resin was treated with TFA at room temperature. After filtration, a solid was isolated from the filtrate using MTBE.

[Preparation Example 4] Production of Aptamer-MNP Conjugate

[0176] FIG. 9 shows a process for producing an aptamer-MNP conjugate (a second binding moiety-carrier conjugate) shown in FIG. 8.

[0177] As shown in FIG. 9, FeCl.sub.2.4H.sub.2O and FeCl.sub.3.6H.sub.2O were washed by repeated heating and cooling in water and dried. MNPs were dispersed using a sonicator. APTES was added slowly to the MNPs and then reacted, followed by drying in a vacuum oven. The completion of coupling was monitored through the Kaiser test. Chloroacetic acid was added to and reacted with the compound, followed by drying in a vacuum oven. Thereafter, an aptamer was linked thereto.

[Preparation Example 5] (1) Production of Peptides Represented by M and Measurement of Retention Time

[0178] In order to confirm the simultaneous detection ability of the detection sensor of the present disclosure, the retention time (RT) for the sequence of each peptide represented by M was measured, and the results of the measurement are shown in Tables 2 to 20 below.A.A

TABLE-US-00002 TABLE 2 SEQ ID A.A sequence RT(Min) 1 LNHEGK 0.867 2 AAATNPAR 0.888 3 SPEDEEK 0.892 4 EGGHNIK 0.894 5 NAGPTAR 0.908 6 FSNSGSR 0.921 7 NDSEPGSQR 0.942 8 TGVIHEK 0.946 9 LVHHNVTR 0.957 10 THHDGAITER 0.965 11 WTNQQK 0.981 12 VNDSGYK 0.984 13 VGSDTVR 0.985 14 VSQALR 0.993

TABLE-US-00003 TABLE 3 SEQ ID Amino Acid sequence RT(Min) 15 ENGTISR 1.012 16 SVDGPIR 1.024 17 FTEPSR 1.024 18 ETFGDSK 1.024 19 HSPGR 1.063 20 NGVHK 1.068 21 NNFGNGR 1.072 22 GDSTFESK 1.077 23 EEQEETSAIR 1.083 24 FQEGQEEER 1.09 25 ILDGGNK 1.1 26 TQTPK 1.117 27 VAHLTGK 1.123 28 VLVEQTK 1.171 29 FDGHR 1.192 30 YHEEFEK 1.209 31 SDFSNEER 1.212 32 ATAGFR 1.246 33 LHGTLPK 1.278 34 SGSGLVGR 1.288 35 AVLIPHHK 1.289 36 SQLANTEPTK 1.291 37 WQHQIK 1.293 38 LIAQASEK 1.295 39 VAQELEEK 1.336 40 EQAALVSK 1.367 41 YVPNSGQEDADR 1.371 42 SADSHGHPR 1.382 43 ISPDR 1.393 44 ASLAEETR 1.42 45 NGNFHPK 1.441 46 LYVVEK 1.453 47 FVTQAEGAK 1.472

TABLE-US-00004 TABLE 4 SEQ ID A.A sequence RT(Min) 48 GSQGAIPPPDK 1.517 49 IQGDLAGR 1.525 50 SVETIK 1.536 51 TIVAK 1.543 52 SHTALLR 1.558 53 SSDANLYR 1.683 54 ELVHTYK 1.687 55 GNVLR 1.72 56 DDVIK 1.754 57 EVFEDSDK 1.776 58 ILADATAK 1.78 59 IAGDQSTLQR 1.834 60 GEAGVIGER 1.862 61 ITQDAQLK 1.863 62 TQVEELSK 1.872 63 GGVASGFK 1.889 64 GAAFVSK 1.896 65 IQTQLQR 1.9 66 IQGDGAALQEK 1.925 67 YIGVGK 1.929 68 FPSTSESR 1.936 69 LNVEGlER 1.94 70 SSALQVSGSTR 1.941 71 EVFENTER 1.954 72 DGPEQLR 1.975 73 VAEAFR 1.994

TABLE-US-00005 TABLE 5 SEQ ID A.A sequence RT(Min) 74 QAFQGAVQK 2 75 SLGDLEK 2.035 76 EVATEGIR 2.038 77 VPPEDIK 2.105 78 ATVVYQGER 2.158 79 VGDVLK 2.166 80 LSSTTTTTGLR 2.166 81 QVFGEATK 2.171 82 SDIAPVAR 2.184 83 GISSTTVTGR 2.197 84 TAATAALAGR 2.204 85 FPDGR 2.225 86 QVPLQR 2.249 87 DADSINSSIDK 2.32 88 ELGYVEAK 2.329 89 VDPHFR 2.36 90 VILDGGDR 2.373 91 AGVGQSWK 2.374 92 TDQYWEK 2.448 93 LTWASHEK 2.448 94 VQDVIER 2.489

TABLE-US-00006 TABLE 6 SEQ ID A.A sequence RT(Min) 95 SGDFYTEK 2.517 96 DQVETALK 2.527 97 SSQAGIPVR 2.545 98 VYSTSVTGSR 2.551 99 STTPASNIVR 2.556 100 ADIIR 2.576 101 TTSDGGYSFK 2.586 102 VFQQVAQASK 2.616 103 ALVVK 2.616 104 EAFAAVSK 2.623 105 EDGSVDFQR 2.662 106 VTFEESAK 2.691 107 IPIQR 2.691 108 SSSISSFK 2.699 109 DLVVQQAGTNK 2.702 110 LPGAHLQR 2.714 111 AHLTVVR 2.718 112 QYTDSTFR 2.742 113 DGHSESSTLIGR 2.841 114 QLTPYAQR 2.887 115 GSGLSLASGR 2.896 116 ELGFGSAK 2.91 117 VTVLGQPK 2.926

TABLE-US-00007 TABLE 7 SEQ ID A.A sequence RT(Min) 118 VAGWGR 3.006 119 QTWVK 3.008 120 TAGGGPDSEL 3.03 QPQDK 121 YSPGGTPTAIK 3.049 122 QHADAVHLISR 3.059 123 LEPQAAVVK 3.078 124 TLLTAAR 3.096 125 LTEATQLGK 3.116 126 SYFEK 3.15 127 AILSTYR 3.252 128 SPYGFR 3.257 129 VLIAHNQVR 3.259 130 VVSYQLSSR 3.278 131 IPGSPEIR 3.287 132 AEQSLQAAIK 3.294 133 SVNAQVTDINSK 3.3 134 ASSFLGEK 3.31 135 DEQVPFSK 3.336 136 ESGVLLTDK 3.425 137 EGYLVK 3.517 138 SVEVLK 3.559 139 ALEQALEK 3.567 140 QWQTLK 3.631 141 DAL SASVVK 3.66 142 VDPVNFK 3.69 143 DGSTIPIAK 3.787 145 TNDPGVLQAAR 3.801 144 FDDESAEEIR 3.801 146 EGTEASLQIR 3.833 147 GGVLIQR 3.834 148 ALNSVAYER 3.904 149 LTQGDYFTK 3.91 150 AGLSTVYK 3.926 151 LFDASDSSSYK 3.971 152 VGVNGFGR 3.978 153 GPGGVWAAK 3.988

TABLE-US-00008 TABLE 8 SEQ ID A.A sequence RT(Min) 154 YEYLEGGDR 4.024 155 YVSALTTPAR 4.025 156 SLLQPNK 4.035 157 GTPPGVYIK 4.062 158 FQASVATPR 4.074 159 QVFAVQR 4.084 160 EIFGQDAR 4.111 161 SVNPYLQGQR 4.114 162 GTFSTTVTGR 4.115 163 LLSEVR 4.127 164 EYFYTSGK 4.132 165 AILGATEVK 4.136 166 VLDEATLK 4.16 167 EQVDQGPDWER 4.162 168 DGPDTLLSK 4.183 169 GWSPTPR 4.194 170 QLYSALANK 4.216 171 VSISTLNK 4.285 172 DFVQPPTK 4.299 173 NAIEALGSK 4.357 174 EDGSLDFQR 4.377 175 DQLVLGR 4.396 176 NANTFISPQQR 4.419 177 SPQAFYR 4.431 178 SGIIIIAIHR 4.448 179 EGSDLSVVER 4.452 180 AVEPQLQEEER 4.486 181 ISSAGASFGSR 4.488

TABLE-US-00009 TABLE 9 SEQ ID A. A sequence RT(Min) 179 EGSDLSVVER 4.452 180 AVEPQLQEEER 4.486 181 ISSAGASFGSR 4.488 182 AWTYR 4.511 183 GGPFSDSYR 4.515 184 VTTNPNLR 4.58 185 DEVEDDYIK 4.582 186 PAPGSTAPPAH 4.594 GVTSAPDTR 187 NQNTFLR 4.602 188 GLGDDTALNDAR 4.61 189 LSVIR 4.64 190 LIQGAPTIR 4.645 191 FPSGTLR 4.66 192 EDAVSAAFK 4.707 193 VAELEDEK 4.739 194 FVGGAENTAHPR 4.742 195 EVASNSELVQSSR 4.751 196 AAISGENAGLVR 4.77 197 TGLQEVEVK 4.775 198 TYLPAVDEK 4.79 199 GGLVDITR 4.798 200 INDISHTQSVSSK 4.807 201 FYQDLK 4.815 202 VEVLVER 4.83 203 LQAEAFQAR 4.852 204 AYTGFEQAAR 4.886 205 TGQIFNQSYSK 4.951 206 HSENFAWTENR 4.956 207 ELGFGSAR 4.961 208 AVIFK 4.972 209 GFVVAGPSR 4.977

TABLE-US-00010 TABLE 10 SEQ ID A.A sequence RT(Min) 210 SNFVPTNVGSK 5.003 211 SLVGLGGTK 5.005 212 VSVYAVPDK 5.007 213 SDIAIDDVK 5.032 214 LGAETLPR 5.033 215 lhAESWYQTK 5.036 216 LVEIVHPSQEEDR 5.037 217 GSYYDSFK 5.039 218 GTYSTTVTGR 5.044 219 IVLVDNK 5.078 220 NPSDEDLLR 5.099 221 ETLDAQTFHTR 5.118 222 QLVEALDK 5.126 223 GEAAGAVQELAR 5.135 224 NFGGGNTAWEEK 5.158 225 GPLQLER 5.183 226 EDLTPFK 5.19 227 IQQNLDQLR 5.226 228 EALFGAR 5.245 229 YTSGFDELQR 5.251 230 LLQEIK 5.265 231 DLETSLEK 5.273 232 YLQSLER 5.283 233 FDPSLTQR 5.284 234 TYSVEYLDSSK 5.318 235 AGFAGDD APR 5.32 236 TLTIQVK 5.321 237 SALTIQTLHTR 5.327 238 SYLPQTVR 5.328 239 YIFTATPAK 5.368 240 VTGVITQGAK 5.379 241 LPTDSELAPR 5.425 242 STDFFQSR 5.426 243 SLYNLGGSR 5.435 244 DTDLDGFPDEK 5.436 245 TFPISGAR 5.447 246 YLLEAK 5.48 247 ELLDYK 5.486 248 IDGVLIR 5.487 249 DISEVVTPR 5.487

TABLE-US-00011 TABLE 11 SEQ ID A.A sequence RT(Min) 250 TTGSGLLK 5.512 251 FDQNLDTK 5.519 252 LWEGSTSR 5.53 253 TNQVNSGGVLLR 5.536 254 LEGEPVALR 5.546 255 SAFSVAVTK 5.552 256 VDGSVDFYR 5.554 257 ETAALNSVR 5.558 258 ESGAEVYFR 5.563 259 FNDTEVLQR 5.568 260 IQALQQQADEAEDR 5.59 261 SLFTEGR 5.591 262 AYPTPLR 5.609 263 ATVFLEQR 5.621 264 EVGQLAETQR 5.624 265 LPVSLSSAK 5.629 266 QLYGDTGVLGR 5.631 267 AEIEYLEK 5.654 268 AAYLSTISK 5.661 269 LTQLNLDR 5.663 270 GQTLLAVAK 5.675 271 VLSFSSR 5.676 272 SLGFVSK 5.683 273 VAQVSITK 5.695 274 GDSVVYGLR 5.7 275 YLQGSSVQLR 5.704 276 DYWSTVK 5.707 277 SESETYTLSSK 5.709 278 ESLAAELR 5.723 279 SNFQQPYITNR 5.73 280 VLQGLPR 5.745 281 NWQDYGVR 5.768 282 DLFDR 5.77 283 ELVYETVR 5.773 284 SELVVEVK 5.782 285 YFQGIR 5.786 286 QINDYVAK 5.789 287 GNPESSFNDENLR 5.79 288 GYFGDEQQIR 5.812 289 VEDIPLAR 5.817 290 NDLISATK 5.823 291 QINDYVEK 5.874 292 EDTPNSVWEPAK 5.874 293 LPPLPPR 5.916 294 FVSTTYSGVTR 5.917 295 DISLSDYK 5.939 296 AAGASVVTELR 5.948 297 TFTPQPPGLER 5.966 298 IPALDPEK 5.995

TABLE-US-00012 TABLE 12 SEQ ID A.A sequence RT(Min) 299 VSSASDYNSSELK 6.007 300 YEIELNLR 6.063 301 LVVVGAGGVGK 6.086 302 DFIYR 6.11 303 YLGEEYVK 6.114 304 LYTLVQR 6.138 305 GQVVYVFSK 6.149 306 LDVDQALNR 6.151 307 LESLLEEK 6.155 308 IIEGEPNLK 6.158 309 GVTSFGLENK 6.161 310 LTISESSISDR 6.164 311 VGDYGSLSGR 6.167 312 EPNAQEILQR 6.172 313 SFLDSGYR 6.179 314 SFHHEESLEELPETSGK 6.182 315 DQYYNIDVPSR 6.186 316 NIDVLEK 6.187 317 DLVQPINPR 6.205 318 INPASLDK 6.213 319 ADVNVLTK 6.216 320 AAGAPLATELR 6.219 321 QSIVPLR 6.223 322 GGSPPAPLPAHLSR 6.229 323 TEFTTALQR 6.234 324 SYVITTSR 6.251 325 DAVEDLESVGK 6.256 326 FLLYNR 6.291 327 QVIDVLETDK 6.339 328 TEEFEVTK 6.36 329 GLQAQGYGVR 6.36 330 ITDFGLAK 6.366 331 LEPESEFYR 6.373 332 ANSFLGEK 6.379 333 GNQWVGYDDVK 6.394 334 DADPDTFFAK 6.421 335 VVTITLDK 6.423 336 DFYVDENTTVR 6.424 337 YLVAPDGK 6.43 338 GSPILLGVSK 6.431 339 DLGSELVR 6.431 340 FSISNANIK 6.466 341 GLLPTSVSPR 6.486 342 YGLHVSPAYEGR 6.491

TABLE-US-00013 TABLE 13 SEQ ID A.A sequence RT(Min) 344 TFYLR 6.529 343 GPGLNLTSGQYR 6.529 345 YPDTLLGSSEK 6.539 346 LSEEEFGGFR 6.555 347 QEYEQLIAK 6.556 348 SLHVPGLNK 6.563 349 TVIEVDER 6.564 350 SLETSAFVK 6.599 351 SDDEVDDPAVELK 6.63 352 AALPEGLPEASR 6.638 353 QLDVEAALTK 6.644 354 LDSSEFLK 6.661 355 AVYEAVLR 6.664 356 VPTPQAIR 6.667 358 VTVNVLSPR 6.669 357 GWDWTSGVNK 6.669 359 FETEQALR 6.698 360 GQDTSEELLR 6.704 361 LSFSYGR 6.719 362 EVSFYYSEENK 6.741 363 APEGFAVR 6.746 364 DYPFQGK 6.75 365 LDGPLPSGVR 6.767 366 FSTQEEIQAR 6.782 367 AYQGVAAPFPK 6.785 368 ISPVEESEDVSNK 6.788 369 YSITFTGK 6.809 370 YQTWIK 6.821 371 QESFFVDER 6.822 372 QQDGELVGYR 6.828 373 FNVSSVEK 6.834 374 TDPGVFIGVK 6.862 375 AAGASVATELR 6.863 376 GEPGEGAYVYR 6.865 377 EAVILYAQPSER 6.87 378 GAVYVYFGSK 6.878 379 YQYAIDEYYR 6.89 380 TELLPGDR 6.89 381 DALEESLK 6.899 382 TEGDGVYTLNNEK 6.904 383 AFLGLQK 6.913 384 SPEAAGVQDPSLR 6.916 386 IQNILTEEPK 6.923 385 GNFVSPVK 6.923 387 DSEYPFK 6.957 388 ENYLLPEAK 6.968 389 DEGSYSLEEPK 6.975 390 VAQGIVSYGR 6.991

TABLE-US-00014 TABLE 14 SEQ ID A.A sequence RT(Min) 391 EQDQVWVR 7.005 392 SVPLPTLK 7.01 393 GNETLHYETFGK 7.02 394 NTQIDNSWGSEER 7.028 395 LLELTGPK 7.031 396 IQELQLAASR 7.039 397 LAAADGAVAGEVR 7.047 398 TAVNALWGK 7.072 399 VGAHAGEYGAEALER 7.076 400 LPGGLEPK 7.093 402 LPGGYGLPYTTGK 7.103 401 LAILYR 7.103 403 QLAEEYLYR 7.134 404 DITSDTSGDFR 7.147 405 AGGSIPIPQK 7.155 406 QNSLLWR 7.159 407 LPASFDAR 7.161 408 QIGEFIVTR 7.172 409 VIDEEWQR 7.18 410 ESDTSYVSLK 7.205 411 SDALQLGLGK 7.221 412 DVAVIAESIR 7.221 413 DSLSINATNIK 7.243 414 LAYYGFTK 7.251 415 GVQINIK 7.273 416 ALLAFQESK 7.28 417 SVIAPSLEQYK 7.301 418 GTHSLPPRPAAVPVPLR 7.304 419 YEELQVTVGR 7.307 420 SQASPSEDEETFELR 7.311 421 YTELPYGR 7.322 422 DFIDIESK 7.323 423 LTPEELER 7.348 424 VTWQNLR 7.356 425 VLDELTLSK 7.378 426 GIDPDLLK 7.384 427 AFVFPK 7.385 428 TAAIVNSIR 7.386 429 NGSQAFVHWQEPR 7.387 430 ELLETVVNR 7.392 431 DLNETLLR 7.405 432 QDGSVDFFR 7.418 433 TSNFNAAISLK 7.419 434 EATLELLGR 7.42 435 AEIYALNR 7.435 436 ALLEAPLK 7.441 437 IELPTTVK 7.46 438 VLFSGSLR 7.461

TABLE-US-00015 TABLE 15 SEQ ID A.A sequence RT(Min) 439 EVEQVYLR 7.51 440 LPGIFDDVHGSHGR 7.516 441 GTPLPTYEEAK 7.522 442 TVPDPLAVK 7.528 443 LQQQLWSK 7.531 444 SQLEESISQLR 7.532 445 QELTTEFR 7.563 446 LYDVLR 7.567 447 TVLFGVQPK 7.568 448 LSVVGYSGSAGR 7.584 449 LFAYPDTHR 7.6 450 ISISTSGGSFR 7.602 451 LSPEYYDLAR 7.604 452 ALPSHLGLHPER 7.628 453 YEVVYPIR 7.644 454 ALFSTLK 7.646 455 IQILPR 7.654 456 SGPTWWGPQR 7.661 457 GLQVALEEFHK 7.665 459 VVGGLVALR 7.676 458 LGDGFEGFYK 7.676 460 VSPLTFGR 7.678 461 TATITVLPQQPR 7.684 462 SANTITSFVDR 7.699 463 NSWGENWGNK 7.71 464 VGDQPTLQLK 7.727 465 ELLEEVGQNGSR 7.736 466 NVIDPPIYAR 7.74 467 VLFYVDSEK 7.741 468 GSEIVAGLEK 7.743 469 GLVVLTPER 7.744 470 AVPEGFVIPR 7.753 471 GWSTDEANTYFK 7.757 472 GVAETPTYPWR 7.763 473 WSGDFTQGPQSAK 7.769 474 LLLGTGTDAR 7.781 475 GLSGIGAFR 7.783 476 ESESAPGDFSLSVK 7.783 477 DFIATLGK 7.798 478 SFISGGSTITGVGK 7.799 479 GVSPSASAWPEEK 7.825 480 DTNALPPTVFK 7.825 481 IFGSYDPR 7.829 482 SLTEILK 7.834 483 TLEPELGTLQAR 7.844 484 SGLSTGWTQLSK 7.849 485 EEADALYEALK 7.856 486 IAQYYYTFK 7.872 487 1EVAQFVK 7.882 488 AELAETIVYAR 7.884 489 FFQYDTWK 7.899 490 LYTDDEDDIYK 7.924 491 DNIYTSEVVSQR 7.937 492 QLVLNVSK 7.954 493 ALDFAVGEYNK 7.963

TABLE-US-00016 TABLE 16 SEQ ID A.A sequence RT(Min) 494 YLGVTLSPR 8.019 495 TTTLPVEFK 8.023 496 TGIIDYGIR 8.067 497 EQPELEVQYQGR 8.069 498 SWSVYVGAR 8.072 499 WVQDYIK 8.115 500 GDLTIANLGTSEGR 8.137 501 DALSALAR 8.148 502 LALFPDK 8.166 503 SGLNIEDLEK 8.176 504 AQATPWTQTQAVR 8.205 505 SLDSPAALAER 8.217 506 YGGDPPWPR 8.221 507 QWAGLVEK 8.239 508 TSFPEDTVITYK 8.24 509 NYNLVESLK 8.253 510 LYIEYGIQR 8.257 511 VEPSVFLPASK 8.288 512 DGGVLSPILTR 8.29 513 VLDELTLTK 8.298 514 LDIGIINENQR 8.308 515 LPEPIVSTDSR 8.313 516 EENDDFASFR 8.344 517 TILFSYGTK 8.369 518 SQFEGFVK 8.376 519 LDPFFK 8.377 520 DSDLLSPSDFK 8.383 521 ALENLLPTK 8.396 522 TIELLGQEVSR 8.399 523 VGYPGPSGPLGAR 8.435 524 NFPSPVDAAFR 8.448 525 YISLLK 8.45 526 IPQEEFDGNQFQK 8.466 527 SAVTALWGK 8.49 528 LSILYPATTGR 8.493 529 LFLETAEK 8.497 530 QLEWGLER 8.498

TABLE-US-00017 TABLE 17 SEQ ID A.A sequence RT(Min) 531 IIVPLNNR 8.503 532 DDFLIYDR 8.515 533 AGYYYIYSK 8.573 534 TPASQGVILPIK 8.599 535 NTVLVWR 8.605 536 IVEELQSLSK 8.612 537 TFYNASWSSR 8.634 538 QEVWLANGAAESR 8.643 539 ISVPYEGVFR 8.654 540 IIDGVPVEITEK 8.674 541 FQLFGSPSGQK 8.675 542 ANVFVQLPR 8.687 543 AQWANPFDPSK 8.698 544 LAAWLAK 8.737 545 YYTVFDR 8.76 546 EFSEENPAQNLPK 8.767 547 FTGSSWIK 8.818 548 IWLDNVR 8.829 549 ETLLQDFR 8.838 550 LTFYGNWSEK 8.849 551 QLVPALGPPVR 8.852 552 ENYPLPWEK 8.869 553 LELQQLQAER 8.879 554 IVIEYVDR 8.897 555 IPVDLPEAR 8.917 556 DPTFIPAPIQAK 8.918 557 QQPLFVSGGDDYK 8.93 558 VLLPPDYSEDGAR 8.937 559 FVSFLGR 8.948 560 FSAEFDFR 8.954 561 DQEAPYLLR 8.984 562 AFLLTPR 8.984 563 WAFNWDTK 8.989

TABLE-US-00018 TABLE 18 SEQ ID A.A sequence RT(Min) 564 STDYGIFQINSR 9.061 565 DSPSVWAAVPGK 9.076 566 VEYITGPGVTTYK 9.123 567 LLPYVLEK 9.131 568 LVIIEGDLER 9.17 569 TVIYEIPR 9.195 570 GPPAALTLPR 9.215 571 TPLYIDFK 9.246 572 NLQEILHGAVR 9.251 573 LLDLGAGDGEVTK 9.27 575 YSSDYFQAPSDYR 9.312 574 DTSLFSDEFK 9.312 576 IPEGEAVTAAEFR 9.316 577 EGYYGYTGAFR 9.322 578 EGHFYYNISEVK 9.322 579 DSTYSLSSTLTLSK 9.328 580 NGSGPFLGNIPK 9.429 581 YGNLSNFLR 9.441 582 GNPTVEVDLYTAK 9.489 583 VYLPWSR 9.49 584 YLPLENLR 9.502 585 VYSGILNQSEIK 9.525 586 FPLTNAIK 9.527 587 VIEASFPAGVDSSPR 9.529 588 TWYPEVPK 9.543 589 QIFLPEPEQPSR 9.584 590 QELIQAEIQNGVK 9.595 591 GDLYFANVEEK 9.684 592 GWVTDGFSSLK 9.711 593 VDAETGDVFAIER 9.715 594 LFQIQFNR 9.752 595 AQDGGPVGTELFR 9.758 596 YGSQLAPETFYR 9.77 597 LSSPAVITDK 9.818 598 AYSLFSYNTQGR 9.818 599 LAILGGVEGQPAK 9.824 600 DWFLR 9.83 601 YSFTIELR 9.849 602 AADDTWEPFASGK 9.876 603 LPGIFDDVR 9.894 604 ELTLEDLK 9.897 605 ESFEESWTPNYK 9.903 606 TSVPPFNLR 9.909 607 DYPDEVLQFAR 9.937 608 WIQEYLEK 9.943 609 FGIILR 9.944 610 FEDGVLDPDYPR 9.952 611 ANLTVVLLR 9.959 612 GSVQYLPDLDDK 9.966 613 LSDLEAQWAPSPR 9.971 614 LPLEYSYGEYR 9.987 615 FNAPFDVGIK 9.988

TABLE-US-00019 TABLE 19 SEQ ID A.A sequence RT(Min) 616 YLYTDDAQQTEAHLEIR 10.055 617 FYTFLK 10.159 618 VPPPSDAPLPFDR 10.215 619 FLNVLSPR 10.31 620 QFYSVFDR 10.319 621 TFTLLDPK 10.331 622 NSSAAWDETLLEK 10.467 623 LALAFYGR 10.524 624 DYVSQFEGSALGK 10.624 625 DSSAAWDEDLLDK 10.652 626 SWSWNYYR 10.694 628 VDLFYLR 10.814 627 ITFSPPLPR 10.814 629 LLWQLNGR 10.817 630 DSSATWEQSLLEK 10.839 631 NPLNAGSWEWSDR 10.935 632 YSVFPTLR 10.973 633 VTAGISFAIPSDK 10.994 634 FLASVSTVLTSK 11.022 635 QSWGLENEALIVR 11.09 636 FLVSLALR 11.108 637 EYFWGLSK 11.156 638 TVDNFVALATGEK 11.297 639 ALAAVLEELR 11.307 640 VGYPELAEVLGR 11.414 641 FTPWWETK 11.516 642 TLAFPLTIR 11.554 643 LPPWNPQVFSSER 11.974 644 SYELPDGQVITISNEWFR 12.048 645 WVAVVFPLSYR 12.064 646 TVAGQDAVIVLLGTR 12.068 647 VLLVELPAFLR 12.103

[0179] As shown in Tables 2 to 19 above, as a result of producing the peptides represented by M and then measuring the retention time (RT) for the sequence of each of the peptides, it was possible to produce various sequences for each retention time (RT).

TABLE-US-00020 A.A NO SEQ ID sequence hydrophobicity RT(Min) 1 SEQ ID 648 LVLK 14.13 2.14 2 SEQ ID 649 TLLK 13.48 1.48 3 SEQ ID 650 SLLK 12.96 1.52 4 SEQ ID 651 IVLK 12.84 1.82 5 SEQ ID 652 LTLK 10.92 1.72 6 SEQ ID 653 LSLK 10.54 1.83 7 SEQ ID 654 LALK 9.88 1.62 8 SEQ ID 655 ITLK 9.64 1.55 9 SEQ ID 656 ISLK 9.25 1.53 10 SEQ ID 657 TVLK 8.22 1.08 11 SEQ ID 658 SVLK 7.91 1.1 12 SEQ ID 659 VTLK 7.49 1.17 13 SEQ ID 660 VSLK 7.25 1.18 14 SEQ ID 661 VLTK 6.43 0.99 15 SEQ ID 662 TALK 5.65 0.98 16 SEQ ID 663 SALK 5.34 0.96 17 SEQ ID 664 KIAVLAI 25.59 9.95 18 SEQ ID 665 KITVLAI 24.86 9.84 19 SEQ ID 666 KIAVLTI 25.39 9.83 20 SEQ ID 667 KIAVLSI 25.39 9.76 21 SEQ ID 668 KISVLAI 24.86 9.74 22 SEQ ID 669 KIATLAI 21.3 8.33 23 SEQ ID 670 KIASLAI 21.3 8.01 24 SEQ ID 671 KIASLSI 20.93 7.84 25 SEQ ID 672 KTTVLAI 19.75 7.44 26 SEQ ID 673 KSAVLAI 19.63 7.11 27 SEQ ID 674 KIAVSAI 18.53 7.1 28 SEQ ID 675 KSSVLAI 18.59 6.92 29 SEQ ID 676 KTTTLAI 15.41 5.97 30 SEQ ID 677 KIAVLTT 19.23 5.91 31 SEQ ID 678 KIAVSSI 16.65 5.84 32 SEQ ID 679 KIAVLAS 17.13 5.27 33 SEQ ID 680 KSASLSI 14.41 5.12 34 SEQ ID 681 KSSSLAI 13.05 4.58 35 SEQ ID 682 KIAVTAT 10.98 2.35 36 SEQ ID 683 KIAVTTT 11.22 2.19 37 SEQ ID 684 KIAVSAS 8.81 1.59 38 SEQ ID 685 KIAVSSS 7.91 1.27 39 SEQ ID 686 KTAVTAT 5.65 1.03 40 SEQ ID 687 KSAVSAS 7.61 0.96

[0180] In addition, as shown in Table 20 above, as a result of additionally producing the peptides represented by M and then measuring the hydrophobicity and retention time (RT) for the sequence of each of the peptides, it was possible to produce various sequences showing a retention time (RT) of 30 seconds to 20 minutes. In order to quantify the same biomarker in multiple samples using the peptide, a binding moiety that recognizes the analyte, such as a detection moiety composed of a different sequence for each sample, may be provided, so that multiple samples may be pooled into one and quantified simultaneously.

[Preparation Example 6] (2) Production of Peptides Represented by M and Measurement of Retention Time

[0181] In order to confirm the simultaneous detection ability of the detection sensor of the present disclosure as described in Preparation Example 5 above, the peptide (TLVPR) represented by SEQ ID NO: 688 and the peptide (SLVPR) represented by SEQ ID NO: 669 were synthesized, and then the retention time (RT) for each of the sequences of these peptides was measured. The results of the measurement are shown in Table 21 below. In addition, these compounds were prepared at a concentration of 1.5 μg/ml, and then the peak intensity of each peptide fragment was determined through the mass-to-charge ratio of each peptide fragment in a mass spectrometer, and the results are shown in FIGS. 10a and 11a; and the magnified peaks are shown in FIGS. 10b and 11b.

TABLE-US-00021 TABLE 21 No SEQ ID A.A sequence RT(Min) 1 SEQ ID 688 TLVPR 8.4 2 SEQ ID 689 SLVPR 8.5

[Preparation Example 7] (1) Synthesis of Units and M

[0182] FIG. 12 shows the kinds of exemplary amino acids or amino acid analogs that may correspond to X.sub.1 to X.sub.m in Formula 2 of the present disclosure. In addition, FIG. 13 shows examples of M that may be obtained by polymerizing these amino acids or amino acid analogs.

[Preparation Example 8] (2) Synthesis of Units and M

[0183] As shown in FIG. 14, a disaccharide that may be M of the present disclosure was prepared. The disaccharide M was degraded by lactase or under an acidic condition into two monosaccharides that are isomers of each other, and thus the sensitivity in mass spectrometry thereof was doubled.

[Experimental Example 1] Experiment for Simultaneous Detection of Four Peptides Represented by M

[0184] In order to confirm the ability to simultaneously detect the peptides represented by M according to the present disclosure, the peptides having the sequences shown in Table 22 below were detected by mass spectrometry MRM, and the results are shown in FIG. 15.

TABLE-US-00022 TABLE 22 No SEQ ID A.A sequence 1 SEQ ID 679 KIAVLAS 2 SEQ ID 672 KTTVLAI 3 SEQ ID 669 KIATLAI 4 SEQ ID 668 KISVLAI

[0185] As shown in FIG. 15, it was confirmed that it was possible to simultaneously detect the peptides having the four sequences shown in Table 22 above.

[Experimental Example 2] (1) Examination of Sensitivity to Peptides Represented by M

[0186] In order to confirm the amplification effect resulting from the repetition of the peptide sequence of the present disclosure, each of the peptide (LTLK) of SEQ ID NO: 652 in Table 20 above and the polymer (LTLKLTLK) composed of two repeats of the peptide was trypsinized, and then the intensity of the peak thereof was measured using a mass spectrometer. The results of the measurement are shown in FIGS. 16 and 17. The mass spectrometer sensitivity (CPS) as a function of the polymerization number was calculated and the results are shown in FIG. 18.

[0187] As shown in FIGS. 16 and 17, compared to the intensity of the peak of the peptide (LTLK) of SEQ ID NO: 652, the intensity of the peak of the polymer (LTLKLTLK) composed of two repeats of the peptide was doubled. In addition, as shown in FIG. 18, it could be confirmed that when the peptide was repeated twice, the sensitivity was exactly doubled, suggesting that when the peptide is polymerized, the sensitivity increases as much as the polymerization number.

[Experimental Example 3] (2) Examination of Sensitivity to Peptides Represented by M

[0188] In order to confirm the amplification effect resulting from the repetition of the peptide sequence of the present disclosure, the peptide fragment (FLK) of SEQ ID NO: 690 or a peptide composed of 2, 4 or 6 repeats of this fragment was produced. Then, each of these compounds was prepared at a concentration of 1 pM, and trypsin was added in an amount of 1:20 to 100 (w/w) with respect to the compound, followed by cleavage into FLK fragments at 37° C. The peptide fragments were dried completely and resuspended, and the mass-to-charge ratio of the FLK peptide fragment was input using a mass spectrometer (MRM mode). The area of the chromatogram was calculated, and the change in the peak intensity as a function of the polymerization number of the peptide fragment was measured, and the results of the measurement are shown in FIG. 19.

[0189] As shown in FIG. 19, it could be confirmed that, when the peptide fragment represented by FLK of SEQ ID NO: 690 is polymerized to form a polymer composed of repeats of the peptide fragment, the detection sensitivity increases in proportion to the polymerization number.

[Experimental Example 4] (1) Evaluation of Diagnostic Ability of Detection Sensor

[0190] In order to evaluate the diagnostic ability of the detection sensor of the present disclosure, a protein detection test was performed as shown in FIG. 20. First, a target protein for cancer diagnosis was selected, and then an aptamer specific to the target protein was prepared, and an aptamer-MNP conjugate was produced in the same manner as in Preparation Example 4. Thereafter, each well was treated with the produced aptamer-MNP conjugate, and each well was treated and reacted with the blood isolated from a person in need of diagnosis. After the reaction was completed, each well was treated with a magnetic field, and a photograph of the blood after treatment is shown in FIG. 21.

[0191] As shown in FIG. 21, impurities other than the target protein that specifically binds to each aptamer could be removed from each well. Thereafter, reaction with each of proteins 1 to 4 through CuCl.sub.2 treatment, removal of the remaining CuCl.sub.2, treatment of each well with the complex compound represented by Chemical Formula 10, and removal of the remaining complex compound were sequentially performed, so that only the [M].sub.n-L.sub.1-N.sub.1-analyte-second binding moiety-carrier conjugate shown in FIG. 22 remained in each well. Then, each well was trypsinized, followed by filtration to obtain peptides.

[Experimental Example 5] (2) Evaluation of Diagnostic Ability of Detection Sensor—Simultaneous Measurement of Multiple Samples

[0192] In order to confirm the diagnostic ability of the detection sensor of the present disclosure, simultaneous quantification of multiple samples was performed in the same manner as in Experimental Example 5, and the results are shown in FIG. 23.

[0193] Protein (albumin) present in human samples was selected. Accordingly, an aptamer specific to the protein was prepared, and an aptamer-MNP conjugate was produced in the same manner as in Preparation Example 4. Next, as in Experimental Example 5, each of wells 1 to 4 was treated with the produced aptamer-MNP conjugate, and then each well was treated and reacted with the blood isolated from a person in need of diagnosis. After the reaction was completed, each well was treated with a magnetic field as shown in FIG. 21. As a result, impurities other than the protein that bind specifically to the aptamer could be removed from each well. Thereafter, reaction with each of proteins 1 to 4 through CuCl.sub.2 treatment, removal of the remaining CuCl.sub.2, treatment of each well with the complex compound represented by Chemical Formula 10, and removal of the remaining complex compound were sequentially performed, so that only the [M].sub.n-L.sub.1-N.sub.1-analyte-second binding moiety-carrier conjugate shown in FIG. 23 remained in each well. M having different sequences were applied to the samples, respectively. Then, each well was trypsinized, followed by filtration to obtain peptides. As a result of analyzing the obtained peptides by a mass spectrometer, the polymer of the detection sensor treated into well 1 was composed of a peptide having a retention time (RT) of 14 minutes, the polymer of the detection sensor treated into well 2 was composed of a peptide having a retention time (RT) of 17.5 minutes, the polymer of the detection sensor treated into well 3 was composed of a peptide having a retention time (RT) of 21.5 minutes, and the polymer of the detection sensor treated into well 4 was composed of a peptide having a retention time (RT) of 24.5 minutes. It could be seen that, for samples 1, 2 and 4, the expression levels of the proteins exceeded the normal reference value, but for sample 3, the expression level of the protein was normal, suggesting that the detection sensor has excellent ability to simultaneously detect an analyte in biological samples with high sensitivity even in simultaneous measurement of multiple samples.

[Experimental Example 6] (2) Evaluation of Diagnostic Ability of Detection Sensor

[0194] In order to evaluate the diagnostic ability of the detection sensor of the present disclosure, albumin was prepared as an analyte and then prepared at concentrations of 0, 0.33 μg/μl, 0.65 μg/μl and 1.3 μg/μl. Thereafter, for the detection of albumin, a complex compound consisting of an albumin-specific peptide (CB3GA)-rhodamine-(SLVPR (SEQ ID NO: 689)).sub.5 having the structure shown in FIG. 24 was produced. Thereafter, the complex compound was allowed to react with albumin in a ratio of 3 to 6 equivalents, and then an unreacted portion of the compound was removed. Thereafter, as shown in FIG. 25, the (SLVPR).sub.5 peptide compound was cleaved into SLVPR fragments by treatment with trypsin, and the change in sensitivity as a function of the concentration of the analyte was measured using a mass spectrometer, and the results are shown in FIG. 27. Meanwhile, for comparison of the diagnostic ability of the detection sensor of the present disclosure, the fluorescence intensity of rhodamine was measured as shown in FIG. 26 before trypsin treatment, and the results are shown in FIG. 28.

[0195] As shown in FIGS. 27 and 28, it could be confirmed that, when the peptide polymer ((SLVPR).sub.5) composed of 5 repeats of the SLVPR peptide fragment was used for albumin detection, the amplification effect could be produced as the peptide polymer was cleaved into 5 SLVPR peptide fragments due to trypsin treatment, and in particular, the sensitivity increased more than 6.5 times compared to that in the fluorescence measurement method.

[0196] As described above, it was confirmed through the Examples of the present disclosure that the detection sensor of the present disclosure could detect the analyte with high sensitivity through amplification, and simultaneous detection was also possible through the production of peptides having various sequences.