3051 GLSRWVEVLALQ GLLRYIDDLTSH NLRCTLFRAWYN VHWDFRQWWQPS 4 Phage display (subtractive panning) 3 PMID:27034429 Kappa fractions of polyclonal immunoglobulin G(IgG) of multiplemyeloma patient MM035 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Screenings were performed after twofold negative selection on polyclonal immunoglobulin G. 3052 SPTPSSSMYTLR WPSSLLTDYPPR DPYQVIWYSHDA MLEPDPYQMTWA 4 Phage display (subtractive panning) 3 PMID:27034429 Kappa fractions of polyclonal immunoglobulin G(IgG) of multiplemyeloma patient MM077 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Screenings were performed after twofold negative selection on polyclonal immunoglobulin G. 3053 THMWVWDVSPEL NGAPLWDMPPHH HFAPWDILPTSK DKLWDIKPLITA AWDWDMPPLRHV SFHWDLRPYSKL SPKPLWDLRPLH 7 Phage display (subtractive panning) 3 PMID:27034429 Kappa fractions mixture of polyclonal immunoglobulin G(IgG) of multiplemyeloma patient MM023 and MM031 and MM041 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Screenings were performed after twofold negative selection on polyclonal immunoglobulin G. 3054 RHLLLNQ(10/15) MTGNHNS(2/15) SFSLKNW(1/15) GERHYPQ(1/15) 4 Phage display (subtractive panning) 3 PMID:27479451 Peptide nanotubes (PNTs) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) The eluted phages were incubated with a SiO2 chip for 1 h, to conduct negative screening of the phages which bind only to this substrate. 3055 CSSAGSLFC 1 Phage display (common panning) 4 PMID:27556860 Anti-human VEGF monoclonal antibody Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) 3056 MHPNAGHGSLMR(3) QGGIPLSRTTFV(1) SLFGCSGICLKA(1) AAFPSLNLRTQP(1) KPGDTAMHYFPP(1) TSTNGKAAILVV(1) DRSHNFWFESGE(1) WDEQARTYPLRS(1) GDGNSVLKPGNW(1) 9 Phage display (subtractive panning) 3 PMID:27336166 Cellulose of paper Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Toner was initially treated with the phage library to eliminate non-specific peptides. 3057 MHPNAGHGSLMR(3) GVILVLLGLCSF(1) SPVAVRSNVFVQ(1) KVPVGVLPLSHS(1) KASGSPSGFWPS(1) MPVKHMPKAHWI(1) DFSMDTHINYRR(1) TPQSFWQKGSLV(1) 8 Phage display (subtractive panning) 4 PMID:27336166 Cellulose of paper Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Toner was initially treated with the phage library to eliminate non-specific peptides. 3058 LPVNGDAELWHS(9) SGVYKVAYDWQH(2) SQDIRTWNGTRS(1) VPTSQAGSGTVT(1) 4 Phage display (subtractive panning) 3 PMID:27336166 The printed toner of standard office laser printers Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Cellulose was initially treated with the phage library to eliminate non-specific peptides. 3059 LPVNGDAELWHS(9) SGVYKVAYDWQH(2) 2 Phage display (subtractive panning) 4 PMID:27336166 The printed toner of standard office laser printers Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Cellulose was initially treated with the phage library to eliminate non-specific peptides. 3060 NRPDSAQFWLHH(6) SMAGEQISWALI(3) VPSIDVSTVSYP(1) GTIQPYPFSWGY(1) WTPTIRTQFVPA(1) QPGHAILAQHPT(1) SARLSMHEMTYL(1) YVNSHSILGYTG(1) TGHLYPTRMEIQ(1) NFTLMNAKTFRW(1) HSDNHYRPADKL(1) EELEWTRKAPMV(1) TDNTMYDKQFQK(1) YPTDWLWHGHNK(1) NASTLPLQKYPT(2) 15 Phage display (subtractive panning) 5 PMID:27582001 Recombinant human prostate-specific membrane antigen (PSMA) extracellular domain (ECD) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Phages from the previous round were incubated with PC-3 cells (PSMA negative) for one hour to remove non-specific bound phages. 3061 NRPDSAQFWLHH(10) YPTDWLWHGHNK(4) HSDNHYRPADKL(3) QPGHAILAQHPT(3) TGHLYPTRMEIQ(2) SMAGEQISWALI(1) GTIQPYPFSWGY(1) YVNSHSILGYTG(1) KLSTTHDRLMLN(1) TVPGDSSPPRLD(1) 10 Phage display (subtractive panning) 5 PMID:27582001 Recombinant human prostate-specific membrane antigen (PSMA) extracellular domain (ECD) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Phages from the previous round were incubated with PC-3 cells (PSMA negative) for one hour to remove non-specific bound phages. The phages from the fourth round were used for in vivo biopanning against xenograft LNCaP tumor. 3062 CKNPTTGTC(14) CGVHSQSSC(9) CSSSPYAWC(6) CWSSFRDEC(4) CNTPMQRSC(3) CSLRGHDLC(2) CTKHTLSIC(2) CKSTPTNGC(1) CPPSKYHLC(1) CPQHFKTFC(1) CITTPGFLC(1) CGEASSPRC(1) 12 Phage display (common panning) 3 PMID:27579674 Anti-carbohydrate larval antigen (CarLA) mAb PAB1 Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) 3063 SVSVGMKPSPRP(19)[1.034] TMGFTAPRFPHY(12)[0.955] SVCVGMKPSPRH(2)[1.127] YVSVGMKPSPRP(1)[1.044] SMGFTAPRFPHY(1)[0.826] SMGLGVPRFPHH(1)[0.532] SVGLGTKRIPHH(1)[0.522] 7 Phage display (subtractive panning) 5 PMID:27609463 Tuberculosis (TB)-positive sera Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The collected phages were used for two rounds of negative biopanning severally targeting TB-negative serum and the blank plate respectively to eliminate non-specific phages. 3064 IQSPHFF[0.88] 1 Phage display (common panning) 3 PMID:27639393 Tyrosinase Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) 3065 TLHPAAD 1 Phage display (common panning) PMID:27555439 Colon cancer cell line SW480 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) According to the results of phage ELISA, phage clone displaying TLHPAAD peptide (SW-TUP clone) showed a significantly higher binding to empty wells than SW480-containing wells. SW-TUP was also found to have a higher binding to empty wells compared with M13KE phage or the whole Ph.D.™-7 library. However, the binding of SW-TUP to SW480-containing wells indicated a slight but insignificant increase compared with both types of control phage clones. These oservations exhibited the TLHPAAD-driven binding of SW-TUP phage to polystyrene. 3066 AEHNPRS AGTTGSL ALAPPVA APAVYLQ APDSGPM APTLVTL ATDASGM DEATSLK DQPAGHL DSARPAS GDLPLAM GLLNPSS IPRDPTT ISPQTGS KVSQPYT MGTYLHG MYTYPIS QHHNPMA QLPHVTQ QPTMQAS RALGPSR SSQPFWS STAHPLP SVTVPPP TAHPILP TASELSR TMQRGAA TPPSLPP TPTISER TSFERSQ VGRAAPL YTTSVRE 32 Phage display (in vivo) 1 PMID:24832468 Glioma-initiating cell, GIC Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) To adapt phage display into anin vivo tumor, we selected a flank tumor model to permit the recovery of a large number relatively pure tumor cells. Bulk glioblastoma cells were implanted into the flanks of BALB/c nu/nu mice. The flank tumor grew until it reached 1 cm in diameter, then the phage display library was injected via the tail vein of the mouse and allowed to circulate and bind to cellular targets for 24 h. 3067 RCQYPLCS(14/40) SCKTVFCY(3/40) RCLRSHCG(3/40) RCPRFSCW(2/40) SCFRPTCP(2/40) RCQYSPCH(1/40) 6 Phage display (common panning) 3 PMID: Fluorescent phosphor LaPO4:Ce3+,Tb3+ (LAP) Not determined. Not determined. Not determined. LX-4 phage display library (XCX4CX) A phage clone containing the surface peptide loop RCQYPLCS was found to bind specifically to LAP. Specificity and affinity of the identified phage bound peptide was confirmed by using binding and competition assays, immunofluorescence assays and zeta potential measurements. Binding and immunofluorescence assays identified the peptide’s affinity for the fluorescent phosphor components CAT and BAM. No affinity was found for other fluorescent phosphor components such as YOX. The binding specificity of the RCQYPLCS peptide loop was improved 3-51-fold by using alanine scanning mutagenesis. The identification of peptides with high specificity and affinity for special components in the fluorescent phosphor in CFLs provides a potentially new strategic approach to rare earth recycling. 3068 VPGWSQAFMALA(21) DTDWVRMRDSAR(9) DMTYMERRDSAR(2) NHVPQHTPIHLR(2) AHVPQHHAMTGR(2) VPGWSQTFMPLA(1) GHVTQHSQRGYS(1) GHVPQHARLLGL(1) THVPEHLLKPRP(1) GHVQQHDVHSIR(1) YHVPEHAVRLGP(1) KHVLQHQTSMTM(1) KHVVQHEYAPNA(1) HHTDEHWLFAKK(1) LSHRTHDRIGFT(1) YPPQERTVHKYV(1) DAYTQLRDRMRQ(1) IDGYPGSPRLPW(1) WHWTWPADVGWV(1) H-V-P-[GQ]-[WH]-S-Q, D-T-x(4)-R-D 19 Phage display (subtractive panning) 3 PMID:27659529 Anti-EGFR monoclonal antibody panitumumab Epidermal growth factor receptor (EC:2.7.10.1) Not determined. Not determined. Ph.D.-12 phage display library (X12) In each round of selection, phage clones were preabsorbed by human IgG immobilized on rProtein A sepharose beads to remove unspecific phages, followed by positive selection with panitumumab counterpart. To enhance the immune responses, we generated recombinant proteins of P19 (DTDWVRMRDSAR) or P26 (VPGWSQAFMALA) fused to a heat-shock cognate protein 70 (Hsc70), and evaluated the efficacy of Hsc70-P19 and Hsc70-P26 as vaccines in vivo. Immunization with Hsc70-P19 or Hsc70-P26 fusion protein stimulated the immune system to produce specific antibodies against peptides as well as EGFR. Moreover, antibodies elicited against mimotopes could induce antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and inhibit the proliferation of EGFR-overexpressing A431 cells. Treatment with Hsc70-P19 and Hsc70-P26 significantly reduced tumor growth in BALB/c transplantable lung cancer models. Although there was no sequence homology between the phage-derived peptides and EGFR by alignments, both peptides mimic the conformational structure of EGFR binding to panitumumab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hage display (common panning) 3 PMID:25989088 Human β-Ⅻa Not determined. Not determined. Not determined. TATA-cyclized CXnCXnC phage display library (CXnCXnC) Inhibition assay The inhibitory activity of bicyclic peptides was determined by incubation with proteases and quantification of their residual activity with a fluorogenic substrate. The inhibitory constant Ki (nM) was calculated and shown. NT denotes not tested. 3070 KCSFREAVCN(13)[NT] ACGRDGFLCQIMRMKCG(2)[>100] ACEMEGWWCTEPVVTRG(2)[NT] VCELWYIVACV(2)[NT] WCAPVFCWWQHCP(2)[NT] YCGELWCWYWMCG(2)[NT] ACKQQGFLCSIATMKCG(1)[>100] YCFPGCAKPCV(1)[NT] WCQDFWCSPVWCL(1)[NT] WCGPWYCMWEGCQ(1)[NT] TCYKFFCGDAVCT(1)[NT] GCWAWFCDYQGCI(1)[NT] WCYGAFCFGQTCF(1)[NT] WCYGGFCWLHWCQ(1)[NT] WCPFMVCWWGTCQ(1)[NT] KCFQGVCYDMWCP(1)[NT] QCCWWFCWDSDCT(1)[NT] MCCTSGCEFQDCY(1)[NT] QCWEPWCCLWLCA(1)[NT] CCLWGFCDQDWCW(1)[NT] CCQELWCYLSFCI(1)[NT] ACNVGDFLCQIQLMKCG(1)[NT] ACQAGEFICAVSANKCG(1)[NT] ACGAQGFLCATSEMKCG(1)[NT] ACENYDFRCAVQVLKCG(1)[NT] ACVKPMFSCFVNQNRCD(1)[NT] ACQPNSGLCWKPVAKCG(1)[NT] ACRTQNPYCQLKQEACG(1)[NT] ACLFMNPYCQVKELMCG(1)[NT] ACQDSVKPCYSAVVLCG(1)[NT] ACRRIQPFCLLLLAVCG(1)[NT] ACQYWDGTCCLSHNSCG(1)[NT] ACDNQCPRCISPWLMCG(1)[NT] 33 Phage display (common panning) 3 PMID:25989089 Anti-ferritin polyclonal antibody Not determined. Not determined. Not determined. TBAB-cyclized CXnCXnC phage display library (CXnCXnC) Inhibition assay The inhibitory activity of bicyclic peptides was determined by incubation with proteases and quantification of their residual activity with a fluorogenic substrate. The inhibitory constant Ki (nM) was calculated and shown. NT denotes not tested. 3071 HPNVPFGVIADG(2)[1.06 ± 0.23] VSDYAFGYWNTL(1)[1.09] GFDIPFGVSLGV(1)[1.29] GSFAMKELYDPF(1)[0.77] QSMASKDLPFGQ(1)[1.31] VVPVDPPFGITW(1)[1.54] DDVPFGRNPAMG(1)[1.45] GNCTLMPPDPPF(1)[1.07] EEPFGTFVDRMA(1)[1.02] EASYPFGYFATA(1)[0.92] ELFDPFGNGLDW(1)[1.25] AISWTDVPFGSK(1)[1.12] TLSSGERAFGSL(1)[1.29] EPAFGLPPMAQK(1)[1.39] SELYKPFGTFRH(1)[1.20] LANNSAEKEYPW(1)[0.90] SALSTGGHDPPF(1)[0.95] ARDYPFGVYHSR(1)[1.12] EASYPFGYFATA(1)[1.31] DPPFGFNHAMY(1)[1.23] SGQATSEVLPPF(1)[1.09] LANNSAEKEYPP(1)[0.92] ERLEIEPSWGF(1)[0.80] NLGGKDPLFGIY(1)[0.76] LANRDPAFGSLS(1)[0.91] E-X-[ED]-P-P-F-G 25 Phage display (common panning) 3 PMID:27824100 Anti-E protein monoclonal antibody (mAb) 3B6 E protein Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The OD450nm value was measured in a microplate Reader. The data shown were reproduced from Figure S1. A minimal B-cell epitope (EXE/DPPFG) that mediates binding to a nonneutralizing monoclonal antibody was identified. It is identical to amino acids 374 to 380 (EVEPPFG) of the E protein of duck Tembusu virus (DTMUV). DTMUV-positive duck serum reacted with the epitope, and amino acid substitutions revealed the specific amino acids that are essential for antibody binding. Dot-blot assays of various flavivirus-positive sera indicated that EXE/DPPFG is a cross-reactive epitope in most flaviviruses, including Zika, West Nile, Yellow fever, dengue, and Japanese encephalitis viruses. These findings indicate that the epitope sequence is conserved among many strains of mosquito-borne flavivirus. Protein structure modeling revealed that the epitope is located in domain III of the DTMUV E protein. 3072 TWTCSDVICTAR(3)[3.14 ± 0.05] SCTSPHCFMWLP(4)[3.34 ± 0.04] TGYICDEMFCKL(1)[3.01 ± 0.05] 3 Phage display (subtractive panning) 4 PMID:27832083 Outer membrane protein U, OmpU Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The OD492nm value was measured in a microplate Reader. In the test, M13 phage in peptide library was used as negative control and TBST as blank control. Each clone experiment was performed in triplicate. The OD492nm of M13 phage and TBST is XX and yy, respetively. The data shown were reproduced from Figure 1. An additional incubation step with His tag protein was added in the first round of panning, and the unbound fraction was used for panning with OmpU. Synthetic OmpU-binding peptides (TWTCSDVICTAR designated P1, SCTSPHCFMWLP designated P2, TGYICDEMFCKL designated P3) were measured for their adhesion antagonistic activity and binding affinity via adhesion inhibition test and non-competitive ELISA, respectively. The results showed that after co-incubated with the mixture of rOmpU and P3, visible green fluorescence could be observed on the epithelioma papulosum cyprinidi (EPC) cells surface; while the EPC cells co-incubated with the mixture of rOmpU and P1/P2 exhibited little green fluorescence. The averagead hesion number of V.mimicus 04-14 isolate before and after treatment with peptide was 21.4±1.5, 20.8±0.8(irrelevant peptide), 20.2±0.5 (P3), 5.1±0.7 (P1) and 3.4±0.8 (P2), respectively. There was a significant decrease in the adhesive level of 04-14 isolate treated with P1/P2 compared to the untreated isolate (p<0.01). The affinity constants of P1 and P2 were (6.17±0.19)e8 L/mol and (1.24±0.56)e9 L/mol, respectively. Furthermore, protective effects of P1 and P2 on grass carps challenged with V.mimicus were preliminary detected. It was found there was delayed death of fish in the groups treated with P1/P2, and the survival rate of challenged fish improved with the increase of the dose of adhesion antagonistic peptide. 3073 ELNLPWQRNALV[1.47] SAENDLTLPWTT[1.14] MANAEIDLPWTK[1.23] HPHDLNDLTSPF[1.13] EFWTALSDPWYF[1.29] AHLHDPFTTLSP[1.00] LDFHDLNRPFNN[1.29] THDPLDSPWNFS[0.99] FNDLDLPFGKRA[1.11] SYDLDLPWIARK[1.08] SFLELDPPWTTN[1.16] QHSFLDLPWHLT[1.08] HPHDLNLPTSPF[1.33] HPHDLNLPTSPF[1.22] MANADLNLPWTK[1.37] TSHSWDLNLPSG[1.43] D-L-[DN]-L-P-W-T 16 Phage display (common panning) 3 PMID:27834908 Anti-E protein monoclonal antibody (mAb) 1F3 E protein Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The OD450nm value was measured. The data shown were reproduced from Figure 1. One minimal epitope was mapped to 221-LD/NLPW-225 and by using phage display and mutagenesis. Duck Tembusu virus (DTMUV) positive duck sera reacted with the epitope, thus indicating the importance of the minimal amino acids of the epitope for antibody-epitope binding. The performance of the dot blotting assay with the corresponding positive sera indicated that 221-LD/NLPW-225 was a cross-reactive epitope for West Nile virus (WNV), dengue virus (DENV), and Japanese encephalitis virus (JEV) and corresponded to conserved and variable amino acid sequences among these strains. The structure model of the E protein revealed that LD/NLPW was located on domain (D) II, which confirmed that DII might contain a type-specific non-neutralizing epitope. 3074 SRNLSYAEYIQI[1.53] GNYSEYIVGKLV[1.19] SSYANYIQFRNT[1.02] SSYTAYIMARGQ[1.19] NSMSEYINYILT[1.25] VDYSTYISRLTS[1.19] NFMNYAEYVQKK[1.45] VDYSTYISRLTS[1.22] TVHSYEEYTARR[1.01] VSPYAEYWLSQM[1.39] WDYNLYIKYVAR[1.12] VDYATYISRLTS[1.40] Y-A-E-Y-I 12 Phage display (common panning) 3 PMID:27834908 Anti-E protein monoclonal antibody (mAb) 1A5 E protein Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The OD450nm value was measured. The data shown were reproduced from Figure 1. One minimal epitope was mapped to 87-YAEYI-91 by using phage display and mutagenesis. Duck Tembusu virus (DTMUV) positive duck sera reacted with the epitope, thus indicating the importance of the minimal amino acids of the epitopes for antibody-epitope binding. The performance of the dot blotting assay with the corresponding positive sera indicated that YAEYI was DTMUV type-specific. The structure model of the E protein revealed that YAEYI was located on domain (D) II, which confirmed that DII might contain a type-specific non-neutralizing epitope. The YAEYI epitope-based antigen demonstrated its diagnostic potential by reacting with high specificity to serum samples obtained from DTMUV-infected ducks. Based on these observations, a YAEYI-based serological test could be used for DTMUV surveillance and could differentiate DTMUV infections from JEV or WNV infections. 3075 CRVDLQGWRRCRR[1.80] CRAWYQNYCALRR[0.61] VPCPYLPLWNCAGK[8.20] 3 Phage display (competitive panning) 2 PMID:27836545 Phospholipid hydroperoxidase glutathione peroxidase (GPX4) mutant, GPX4mu Not determined. Not determined. Not determined. CX7-10C T7 phage display library Surface plasmon resonance (SPR) SPR biosensing experiments were performed on a Biacore T100 instrument (GE healthcare).The dissociation constants KD (μM) were shown. Biotinylated Avi-tagged GPX4mu was immobilized to Dynabeads M280-streptavidin (Invitrogen, CA, USA). After one panning agaist SUMO-tagged GPX4mu, the phage libraries were re-panned against SUMO-tagged GPX4mu in the presence of 50 μM SUMO-tag binding synthetic peptides identified from the first panning. The first GPX4 inhibitory peptide, VPCPYLPLWNCAGK, was identified. By analyzing the X-ray crystal structure of the peptide, we found the peptide binds to near Sec73 of catalytic site. This peptide may contribute to developing GPX4-targeted drugs.