1851 TMRGKKKRTRAN(1) QHRMASMSPTLP(1) GLLPYRPREANF(1) AMIPYTWFSPSP(1) KQPKKAPRRIPQ(1) SIPTTWFHPPPS(1) GVSLHNTNWNIY(1) SDTSVNWLTLWY(1) NTPQRPPYKRSP(1) LAKSPSNSAREW(1) AKCHSDVPSPAC(1) VHFKPTHLPSPP(1) STSQALSRFPSF(1) GMMRALSHPSAS(1) GTLTTPRLDLIM(1) MKISAPALAFGL(1) MFAKSPPYPSLM(1) FNWHWLSRPYFP(1) FANHLTNAVHAL(1) SQPWTNALVVSS(1) KLWNVPWPPHMR(1) FTPPPAYGRNEG(1) TAFWPLYPLSDW(1) HWIPQTLPASFI(1) HHPFVTNTPSLI(1) PNRLGRRPVRWE(1) HWWYPLLPVRQM(1) 27 Phage display (common panning) 3 PMID:21926473 EWS-Fli1 protein RNA helicase A, RHA Not determined. Not determined. Ph.D.-12 phage display library (X12) The cytotoxicity evaluation of these peptides with in EWS-FLI1 containing cell lines yielded one potent peptide called ESAP1 (TMRGKKKRTRAN). ESAP1 binds EWS-FLI1 with 0.202 micromolar affinity as measured in surface plasmon resonance. The minimal interaction region of ESAP1 is characterized and found that the lysine residues are critical for cellular cytotoxicity. ESAP1 reduces the transcriptional activity of EWS-FLI1 as well as disrupts cell cycle kinetics in ewing tumor cells. these findings provide both a novel experimental probe and a potential therapeutic scaffol d for ewing tumor. 1852 GAMHLPWHMGTL 1 Phage display (subtractive panning) 3 PMID:21928455 Zinc oxide, ZnO Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The phages were first incubated with the zinc precursor (zinc nitrate solution) at room temperature. Careful selection of the Zn precursors is important for this method. If conventional Zn precursors that form zinc hydroxide solids in aqueous solution are used, amorphous Zn(OH)x might grow in addition to ZnO nanoparticles in the phage solution, and then the panning process could also contain the sequences of peptides that bind amorphous Zn(OH)x nanoparticles. The results suggest that the GAMHLPWHMGTL peptide can not only nucleate the catalytic growth of semiconductor nanoparticles, but can also induce the anisotropic coagulation of primitive crystalline domains at room temperature to form single-crystalline nanoparticles easily and without the need to add complex capping reagents. 1853 DRYSEIRTSSTL(6) YSGLQDSSLRLR(4) DYPSANKWPRYV(1) 3 Phage display (subtractive panning) 3 PMID:21930161 The tegument of schistosoma japonicum schistosomula Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Western blot To confirm the binding ability of positive phages, the MppZL1 (DYPSANKWPRYV), MppZL4 (YSGLQDSSLRLR), MppZL6 (DRYSEIRTSSTL) and negative control M13KE phage were tested for recovery rate. Significantly higher binding was observed by MppZL4 to schistosomula than by MppZL6 or MppZL1 or control M13KE phage. The results of Western blot indicated that the peptide of the MppZL4 exhibited strong affinity for the surface membrane or tegument of schistosomula. Cercariae was directly used for construction of a reverse adsorption peptide library. Of the three, M13 phage peptide ZL4 (MppZL4, YSGLQDSSLRLR, 1.4 kDa, pI 8.8) bound to the tegument of mechanically transformed schistosomula and to other developmental stages of S. japonicum from the mammalian host. By contrast, MppZL4 did not bind to the surface of cercariae. 1854 DFSVLQTIGDSL(0.4) 1 Phage display (competitive panning) 3 PMID:21953453 BH3 motif of Mcl-1 protein 26-amino acid Bim peptide Not determined. Not determined. Ph.D.-12 phage display library (X12) 1855 DFSVLQTIGDSL(0.2) NETVNTMLTYYY(0.2) NETVELMQAYLH(0.2) 3 Phage display (competitive panning) 3 PMID:21953453 BH3 motif of Mcl-1 protein Sabutoclax Not determined. Not determined. Ph.D.-12 phage display library (X12) 1856 CGTFAHPQC(1) CGTFIHPQC(4) 2 Phage display (common panning) 3 PMID:16258189 Streptavidin Biotin 1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5, Not determined. Ph.D.-C7C phage display library (CX7C) 1857 CGTFAHPQC(5) CGTFDHPQC(3) 2 Phage display (common panning) 3 PMID:16258189 Streptavidin Biotin 1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5, Not determined. Ph.D.-C7C phage display library (CX7C) 1858 ACTTHPQNKPKEQRCL AADKWSHPQNPLRSPTMA AADKWSHPQAPVPLLRPA YTTAHPQGDLSV HCMSAHPQDLCT 5 Phage display (common panning) PMID:15620878 Streptavidin Biotin 1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5, Not determined. Not determined. 1859 HGMASQYFTCFHDSEPSSPGMFGWDPTTPTLPHPQVDE IAHRVVAYNSLDSNPIWLPGEESSSVFGDYHPMFRAPV HVPVFTRYNYAKPNDTDWPGGFVDSLSAHPQGPIAGGR MTLGYDRASPAPNTSFSNPGLDFNPFTYHPQGPHQILQ AGRAARDDDCRGHACMIIPGVSLFNSDHPMGAHPSIRR DFSSFLTGTNAMAPFWPFPGSTYLLGHPMAPRDLQTSN SASWKFNSSFGYPTGGIEPGPNCHPQACPDVALKSLSP VSEMSSFSGCNTDHHPQGPGGRHDIMRSISESRGYGSL EMLTLPLTSIPIPWHPQGPGYLYHKPPRGTDFRMLSSK PYRFYHPYSHPRHPQGDVPGSSAEVFHTFPNTQGRNSR ADYGTIGESPCHPQVDICPGALHHEFNEFFVGMSPEPS ARMAGLTEHPQGDIIDHHPGWVHDSKISPRNQDTYHSS AHLFGHPQVGFDSIGSAFPGDIHCKQYKADSGLQSAAA PDYDLMSSTCRFYGCSKMPGGVAVNGLFAVQGHSKYSS TWDFTRSSLPAGDTSFTFPGSYSVMTRSCGISCVPAEV H-P-[QM] 15 Phage display (common panning) 3 PMID:8508960 Streptavidin Biotin 1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5, Not determined. TSAR-9 phage display library (X18PGX18) SA selected two classes of phage from the library. One class exhibited the aa motif, HP(Q/M)Θ (where Θ signifies a non-polar aa), similar to the motif identified by Devlin et al. [Science 249 (1990) 404-4061 using a 15-aa random peptide library displayed on phage. The other class of phage had no discernible motif. In binding experiments, the non-HP(Q/M)Θ phage had a slightly higher affinity for SA than did the motif phage. Both classes of SA-binding phage failed to bind native and non-glycosylated forms of avidin, even though SA and avidin are structurally similar and both proteins possess extraordinary affinities for biotin. 1860 DVDMGTIFNTIANNITSRPGVSWGGSTRTITKPKGAVA AQTAGQPGRTLSKPPIPNTPGPREPSLLHSMPHLPNLTA VRTISKPVAREGWTRDTVPGPATSIVEKRFHLIGVNAQ KGASFYPQCGGECQIYRVPGDHLPLFSLHRTGTPRHDS 4 Phage display (common panning) 3 PMID:8508960 Goat anti-mouse IgG (Fc) polycloanl antibody Mouse IgG Fc Not determined. Not determined. TSAR-9 phage display library (X18PGX18) The polyclonal goat anti-mouse IgG Fc Ab preparation selected phage displaying sequences similar to a region of the mouse IgG Fc. Thus, a single immunodominant epitope on the mouse IgG Fc was identified. 1861 CRLALGDAKKYC[0.180 ± 0.001] CVRKGGLIKGRC[0.153 ± 0.002] CGPRDRGGLIKC[0.130 ± 0.002] CDSNRGGLWRKC[0.158 ± 0.010] DRGGL 4 Phage display (common panning) 4 PMID:17975163 Anti-CEA monoclonal antibody Col-1 Carcinoembryonic antigen-related cell adhesion molecule 5 Not determined. Not determined. CL10 phage display library (CX10C) ELISA In ELISA, phage clones were bound by coated anti-CEA antibody Col-1 and detected by a peroxidase-labeled rabbit anti-phage antibody to determine specificity of peptides. Absorbances at 450-630 nm were determined, reproduced from the graph and shown as means ± standard deviations. The absorbance for negative control was 0.020. No phage binding occurred to isotype control antibody. According to the results of phage ELISA, all of the four independent phage clones bearing above peptides were specifically bound by the antibody Col-1 but were not recognized by an isotype control. No reactivity was observed with the wild-type phage. The competitive ELISA evidenced that the selected mimotopes were true mimics of the Col-1 epitope on the CEA antigen and clone bearing CRLALGDAKKYC peptide was the best circular mimotope candidate. 1862 DRGGLMKTN[0.169 ± 0.003] DMGGLFRKG[0.288 ± 0.004] DRGGLWKTP[0.141 ± 0.005] DRGGL 3 Phage display (common panning) 4 PMID:17975163 Anti-CEA monoclonal antibody Col-1 Carcinoembryonic antigen-related cell adhesion molecule 5 Not determined. Not determined. LL9 phage display library (X9) ELISA In ELISA, phage clones were bound by coated anti-CEA antibody Col-1 and detected by a peroxidase-labeled rabbit anti-phage antibody to determine specificity of peptides. Absorbances at 450-630 nm were determined, reproduced from the graph and shown as means ± standard deviations. The absorbance for negative control was 0.020. No phage binding occurred to isotype control antibody. According to the results of phage ELISA, all of the four independent phage clones bearing above peptides were specifically bound by the antibody Col-1 but were not recognized by an isotype control. No reactivity was observed with the wild-type phage. The competitive ELISA evidenced that the selected mimotopes were true mimics of the Col-1 epitope on the CEA antigen and clone bearing CRLALGDAKKYC peptide was the best circular mimotope candidate. 1863 RGGRCLLCCLCLWWA AVAGGRSVVDARVAR RTEVPVLSFTSPLTG PFARAPVEHHDVVGL RVPPRYHAKISPMVK 5 Phage display (subtractive panning, in vivo) 3 PMID:20692225 Human DA-MB-435eb.1 tumor xenografts Not determined. Not determined. Not determined. f3-15mer phage display library (X15) Before positive selections, the library was subjected to negative selection by passage through non-tumor-bearing mice. Following in vivo selection from the f3-15mer phage display library in mice harboring tumor xenografts, two phage clones (RGGRCLLCCLCLWWA and AVAGGRSVVDARVAR) predominated in final outputs. These clones had no discernible affinity for the tumor cell line in vivo or in vitro but had unusually high infectivities, prompting further investigation. 1864 CWWLHPTHC(17) CPRTHYAIC(3) CAVCTDFC(1) CHLFTQAFC(1) CALFKPSMC(1) CQTSAMRHC(1) CSLNPSSRC(1) CYFNQPIRC(1) CLTLNGSPC(1) CSSKTSFTC(1) 10 Phage display (common panning) 4 http://acta.chem-soc.si/56/56-3-712.html Phospholipase A2, ammodytoxin C Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1865 HWWSPWPNPPQI(3) HWNVWWPVSIPE(1) HSWSFFWQSPAD(1) HSYWYRWTPSHL(1) FHWRWSTFPEYP(1) HWRWWQSDHLFT(1) SHWIRYFPWSIG(1) 7 Phage display (common panning) 4 http://acta.chem-soc.si/56/56-3-712.html Phospholipase A2, ammodytoxin C Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1866 CHSNRLNLC(3) CNGMYAHPC(3) CNMTQAYSC(1) CYRQASDSC(1) CQLQPTRLC(1) CDHHTYNHC(1) CHSPTRGIC(1) CKDSSLHVC(1) 8 Phage display (common panning) 4 http://acta.chem-soc.si/56/56-3-712.html Pancreatic phospholipase A2 Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1867 KLWNLHPTQALW(2) APWHLSSQYSRT(2) GPSVGVTASHTR(1) SNHPATLTGTGG(1) AQPYPFSTRHWQ(1) 5 Phage display (common panning) 4 http://acta.chem-soc.si/56/56-3-712.html Pancreatic phospholipase A2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1868 CLFHHQASC(2) CTARSPLLC(2) CQVPRSPYC(1) CTTRTMTQC(1) CSMSTTRSC(1) CLETASNYC(1) CTSAPHRMC(1) CLPSRSHLC(1) CFWQSDKIC(1) 9 Phage display (competitive panning) 4 http://acta.chem-soc.si/56/56-3-712.html Pancreatic phospholipase A2 MJ33 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1869 HGWLYPHPRYPV(16) HLWPFYSMPPQH(2) HPPYWYPWQQSS(1) 3 Phage display (competitive panning) 4 http://acta.chem-soc.si/56/56-3-712.html Pancreatic phospholipase A2 MJ33 Not determined. Not determined. Ph.D.-12 phage display library (X12) The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. 1870 YAPWNIPLHMYL(3) FHKNWPIWWYPP(3) KLGDPKIATTLF(1) IPHPKLGDPRPM(1) SVTKLGDPRAPR(1) EQMSWMQLLVEM(1) SSRTKLIYQAAS(1) EQMSVAQFTRA(1) STSNYASASSPN(1) NNLIAAFLRTPI(1) FHKNWPIWWYPP(1) WHWYWQPAARGN(1) NPLHAASTIWWF(1) IVLPLSAPTALK(1) TRAAVLISSTWI(1) THRLDNSYSRMS(1) K-[LPV]-G-D-P-[RKL] 16 Phage display (common panning) 3 PMID:21764227 Rabbit anti-PrV polyclonal antibody IgG Pseudorabies virus, PrV Not determined. Not determined. Ph.D.-12 phage display library (X12) Groups of six C57BL/6 mice were immunized with bacteriophages expressing peptides with this motif sequences. Some of the mice were found to be positive in seroneutralization assay; in a challenge setting, all but two immunized mice survived, albeit presenting some disease symptoms. 1871 CKPGDPRHC(1) CKPGDPRQC(1) CKPGDPRSC(1) CKAGDPRTC(3) CKVGDPLRC(1) CKVGDPLWC(1) CKLGDPLAC(3) CKLIRPAVC(1) CLICDAKWC(3) CSFAPQFAC(1) CLLVWWAIC(2) K-[LPV]-G-D-P-[RKL] 11 Phage display (common panning) 3 PMID:21764227 Rabbit anti-PrV polyclonal antibody IgG Pseudorabies virus, PrV Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Groups of six C57BL/6 mice were immunized with bacteriophages expressing peptides with this motif sequences. Some of the mice were found to be positive in seroneutralization assay; in a challenge setting, all but two immunized mice survived, albeit presenting some disease symptoms. 1872 LLPGQTTLATGL 1 Phage display (common panning) 3 PMID:21764227 Rabbit anti-PRRSV polyclonal antibody IgG Porcine reproductive and respiratory syndrome virus, PRRSV Not determined. Not determined. Ph.D.-12 phage display library (X12) 1873 SVSVGMKPSPRP(17)[131.1 ± 7.2] FPTRFKKQWSLP(7)[26.7 ± 3.2] WHKSEQGPRLYR(6)[224.2 ± 39.4] FSRPPARHQPHQ(4)[11.5 ± 4.9] FNLPLPSRPLLR(3)[7.5 ± 0.7] HPLCTSHAPVPP(2)[104.0 ± 40.2] NAGDNKFVRVSP(1)[70.5 ± 6.3] 7 Phage display (common panning) 4 PMID:21979823 CD44 antigen protein Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA Binding affinity was determined by ELISA. The Kdapp value (apparent dissociation constant, pM) was obtained from a binding saturation curve obtained from data derived from three independent experiments and shown. Among these, P7 (FNLPLPSRPLLR) was further characterized. Initially, binding affinities of synthesized P7 peptides were assessed by ELISA or fluorescence microplate reader. And the P7 peptide was exhibited a high specificity for CD44, with a low Kd value. 1874 CGLHPAFQC(28) CSMNQPTAC(16) CPHNTTASC(11) CSSHLSSSC(10) CGPIVHSNC(6) CHLPPTIBC(6) CQWSVYNNC(6) CHQVFGAYC(4) CNSLVPPSC(4) CLSHPPTMC(2) CKSETLLSC(2) CHLRAPLLC(2) 12 Phage display (in vivo) 3 PMID:21999821 Rat visceral adipose tissue Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Adipocyte-specific affinity and transdermal activity of the TDA1 (CGLHPAFQC) were validated in vitro and targeting ability of the dermally administered TDA1 to visceral adipose tissue was also confirmed in vivo. TDA1 was effectively translocated into systemic circulation after dermal administration and selectively targeted visceral adipose tissue without any preference to other organs tested. Fluorescent microscopic analysis revealed that the TDA1 could be specifically localized in the hair follicles of the skin, as well as in the visceral adipose tissue. Thus, the authors inferred that dermally administered TDA1 would first access systemic circulation via hair follicles as its transdermal route and then could target visceral fat effectively. The overall results suggest that the TDA1 peptide could be potentially applied as a homing moiety for delivery of anti-obesity therapeutics to visceral fat through the convenient transdermal pathway. 1875 CTQRPDKSC(0.25) 1 Phage display (subtractive panning) 5 PMID:22002548 Hsp70-peptide complexes, Hsp70-PCs Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Hsp70-PCs were obtained from the human breast carcinoma cell line MDA-MB-231 using ADP-agarose affinity chromatography. Phages interacting with the HSP70 moiety of the HSP70-PC were removed using a subtractive biopanning step with recombinant HSP70.