3076 TTFNSFGRVRIE(2) TTFNSFGRVAIE(1) TTFCSFGRVRIE(1) TTFNSFGRVHWE(1) TTFNSFGKVRIE(1) TTYNSFGRVRIE(1) TTEYSFGRTSTL(1) DTFNSFGRVRIE(1) TTFNSFGRVRIQ(1) TNFNDFKRVRGE(1) TTFSSFGRVRIG(1) TTFNSNGRVWIE(1) TTFNSFGRVRGG(1) TTFNSFYRVRIE(1) 14 Phage display (common panning) 8 PMID:27842517 Human breast cancer cell line MDA-MB-231 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 3077 PRLNVSP(2) PRLNTSP(1) PTLDVAP(1) PQLNVSP(1) PGAQVSP(1) PRTNVAP(1) PRKTVSP(1) PAMNVSP(1) PQENASP(1) PSLNVSP(1) ARLNVAP(1) TMLMVRP(1) ARLNTQP(1) PMMAVAP(1) 14 Phage display (common panning) 8 PMID:27842517 Human breast cancer cell line MDA-MB-231 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) 3078 PRQNQSP QLKNVTP PRLNVAT PRLNVTT PRWAVSP PRLNHSP PQMTAMP MFLNGAP TRLQVSP WRMAHSP 10 Phage display (subtractive panning) 8 PMID:27842517 Human breast cancer cell line MDA-MB-231 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Screening of the phage library was performed by the BRASIL method. In the final round of panning, bound phages from the previous round were incubated with MCF-10-2A cells (non-tumorigenic), which in this case was the aqueous phase containing the phages that did not bind to the control cells. 3079 WWFNSFGRVRIE(4) WAFNSFGRVRIE(1) WWFNKFGKVRIE(1) IWFNSFFRVRIE(1) WWFFSFGRVRIE(1) GWFNSFGRWSWL(1) WWFFSFGRWSWL(1) 7 Phage display (subtractive panning) 8 PMID:27842517 Human breast cancer cell line MDA-MB-231 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Screening of the phage library was performed by the BRASIL method. In the final round of panning, bound phages from the previous round were incubated with MCF-10-2A cells (non-tumorigenic), which in this case was the aqueous phase containing the phages that did not bind to the control cells. 3080 CTDKSKAGFEC(3/100) CSHDSKLWC(3/100) CKDETKYGC(3/100) CKSDAEWFC(3/100) CPKRISKRC(2/100) CIFISKRIC(2/100) CVITNDPDC(2/100) CWVGLDPDC(2/100) CNEDGLHIC(2/100) CGLKHNEDC(2/100) CHTYLTSTC(2/100) CFLTSDEAC(2/100) CTDRWQKIC(2/100) CASWQKITC(2/100) CPITHWRVC(2/100) CDCGATDGC(2/100) CHHTPAANC(2/100) CRTRFKGCC(2/100) CVSHNDPDC(1/100) CVFDDNGRC(1/100) CRENDNGSC(1/100) CWYTGNGNC(1/100) CRGQRNGWC(1/100) CGQRYEPLC(1/100) CCGVSDTEC(1/100) CCGANQEYC(1/100) CSAKSTYPC(1/100) CCPAIWFTC(1/100) CIVSEWRDC(1/100) CPTISEKNC(1/100) CREFYLSDC(1/100) CSGHPEYLC(1/100) CSGHPEYLC(1/100) CGADEEKLC(1/100) CPEDDFLGC(1/100) CPEDDFGLC(1/100) CVNQNDRMC(1/100) CDTSDQNRC(1/100) CHTEVGCNC(1/100) CMTCPPWFC(1/100) CYPCSGPEC(1/100) CHLCSTVGC(1/100) CPGSATCMC(1/100) CLEFTSAGC(1/100) 44 Phage display (subtractive panning) 3 PMID:27845058 IgGs of horse immunized by the crude venom of the Hemiscorpius lepturus Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) The phage-displayed random peptide library was first screened with non-immunized horse IgGs. The unbounded phage (in the supernatant) was screened with the IgG of the immunized sample. 3081 FVRVHTRSSWRVP[0.26] GVWYTDIRMRDWM[0.032] 2 Phage display (common panning) 6 PMID:27856253 BTB domain of B cell lymphoma 6(5-129) BCL-6 corepressors BcoR, SMRT, and N-CoR 1R2B(196), 1R2B(196), X13 T7 phage display library ELISA These peptides exhibited BCL6-selective inhibition in a peptide concentration dependent manner, and the IC50 values (nM) were estimated. 3082 SGADGLVPRQRA[0.73 ± 0.02] VTEADGLVPRNL[1.14 ± 0.03] AHIVSLDDDSTI[0.89 ± 0.02] YSLDDDSTISLN[1.12 ± 0.03] SRDFAPDPTLLM[1.03 ± 0.03] ADGLVPR,SLDDDSTI 5 Phage display (common panning) 4 PMID:27863546 Anti-rVMH-HD polyclonal antibody Not determined. 3BIM(196), 3BIM(196), Ph.D.-12 phage display library (X12) ELISA The binding activities of the positive phage clones to the anti-rVMH-HD antibody were measured by phage ELISA. The OD450 nm values were measured. The data shown were reproduced from the Figure 4 in the reference. 3083 THVSPNQGGLPS(57)[735.2 ± 53.6] TIDNFFSASLRN(13)[NT] THVSPNQGGLRN(1)[NT] 3 Phage display (subtractive panning) 7 PMID:27862961 Hepatocellular carcinoma cell line HepG2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The absorbance at 450 nm of the 96-well plate was measured in microtiter plate reader (Thermo Scientific, USA). The apparent Kd value (nM) between biotin-THVSPNQGGLPS and the human recombinant GPC3 protein was calculated and shown. NT denotes not tested. The target is glypican-3 (GPC3) abnormally expressed in hepatocellular carcinoma (HCC). In the first round, PC3 cells were used in negative screening to eliminate non-specific binding clones. Panning procedure was slightly altered in the seventh round by using human recombinant GPC3 protein for competing off the GPC3 binding peptide instead of Tris-HCl. The ability to target GPC3 in vivo is evaluated by intravenous injection of THVSPNQGGLPS (named as GBP) labeled with a near-infrared dye, Cy5.5, into a HCC tumor-bearing mouse model. Significant high tumor accumulation (tumor/muscle ratio: 6.49 ± 0.55) of Cy5.5-GBP in HepG2 tumors is observed compared with that of the low GPC3 expressing prostate cancer cell line, PC3 (tumor/muscle ratio: 1.15 ± 0.32). By targeting GPC3, GBP differentiates tumor tissues from normal liver tissues in patients, suggesting a great clinical translation potency of GBP. Collectively, GBP demonstrates great potential for HCC detection via fluorescent imaging or histological staining. 3084 GEEFSQLHAFEQDIFSC(46) GEAHCKHSEQDICAIAN(4) GVQRSEQDIFTEPEAHD(2) GHQACEVVQTEGFLLHY(2) GQLVCPHVQTEGECVSC(2) GKDSCVSRVQTEGLAVD(1) GRINSGSRQTEGRYGTY(1) GWWFSVLLTQTEGRKQC(1) GAHTCIFQTEGRIHPQF(1) GHRPCVPATEGRQAAHD(1) GTWNSQQTEGRGSDNCA(1) 11 Phage display (competitive panning) 2 PMID:30267550 Serum 13006 from patients sensitized to soy bean Not determined. Not determined. Not determined. ENTE-1 phage display library (GX3[C/S]X12) A trinucleotide‐based, 16mer peptide phagemid library covering >e9 clones (“ENTE‐1”) was used for two rounds of panning against individual serum from patients sensitized to soy bean. We coated 24 μg total serum protein in 2.5 mL PBS to Immuno Tubes (MaxiSorp™; Thermo Fisher Scientific, Waltham, MA, USA) for 1 hour at 4°C under constant agitation. Under these conditions, all Ig molecules should be bound on the tube surface. A negative control was incubated with PBS only. The coated tubes were washed with 2.5 mL blocking buffer once (5% [w/v] non‐fat dry milk powder in PBS) and incubated with 4 mL blocking buffer at 4°C for at least 15 minutes under constant agitation. Before adding the ENTE‐1 peptide phage display library, the tubes were washed three times with 4 mL PBS. To preferably select patient-specific antibodies, and in particular to prevent selection of peptides binding serum proteins, a competition with a mixture of ten sera from healthy donors was conducted. The ENTE‐1 library was added to each tube in 1 mL blocking buffer containing 30 μg of non‐allergic serum protein. In the first selection round, an amount of phage corresponding to 4e11 colony forming units (cfu) of ENTE‐1 library and in the second selection only e9‐e10 cfu of recovered phage were used. Tubes were incubated for 2 hour at 4°C with constant agitation, washed five times with 1 mL 0.1% (v/ v) Tween 20 in PBS in the first selection round, and with 0.5% (v/v) Tween 20 in PBS in the second selection round. 3085 GGEASIPDIFVQTEGFI(36) GTVVCFIWWPAGYPVDC(6) GSVPSKRFQTEGREQII(4) GGVHSQDYENVQTEGIF(2) GIDGCPITVQTEGQGPD(1) GSGPSSATQVVQTEGQD(1) 6 Phage display (competitive panning) 2 PMID:30267550 Serum 14011 from patients sensitized to soy bean Not determined. Not determined. Not determined. ENTE-1 phage display library (GX3[C/S]X12) A trinucleotide‐based, 16mer peptide phagemid library covering >e9 clones (“ENTE‐1”) was used for two rounds of panning against individual serum from patients sensitized to soy bean. We coated 24 μg total serum protein in 2.5 mL PBS to Immuno Tubes (MaxiSorp™; Thermo Fisher Scientific, Waltham, MA, USA) for 1 hour at 4°C under constant agitation. Under these conditions, all Ig molecules should be bound on the tube surface. A negative control was incubated with PBS only. The coated tubes were washed with 2.5 mL blocking buffer once (5% [w/v] non‐fat dry milk powder in PBS) and incubated with 4 mL blocking buffer at 4°C for at least 15 minutes under constant agitation. Before adding the ENTE‐1 peptide phage display library, the tubes were washed three times with 4 mL PBS. To preferably select patient-specific antibodies, and in particular to prevent selection of peptides binding serum proteins, a competition with a mixture of ten sera from healthy donors was conducted. The ENTE‐1 library was added to each tube in 1 mL blocking buffer containing 30 μg of non‐allergic serum protein. In the first selection round, an amount of phage corresponding to 4e11 colony forming units (cfu) of ENTE‐1 library and in the second selection only e9‐e10 cfu of recovered phage were used. Tubes were incubated for 2 hour at 4°C with constant agitation, washed five times with 1 mL 0.1% (v/ v) Tween 20 in PBS in the first selection round, and with 0.5% (v/v) Tween 20 in PBS in the second selection round. 3086 GSAPALPVEAPK(14)[743.2 ± 69.5] KMPKENPSSWLS(13)[135.8 ± 8.8] GSAPLLTVDTSP(11)[626.1 ± 40.1] SGVYKVAYDWQH(2)[300.4 ± 30.09] 4 Phage display (common panning) 4 PMID:27721007 Prominin-1 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA Activities of phages to the CD133 were measured by phage ELISA. The OD values at 450 nm were measured. The data shown were the Kdapp value (apparent dissociation constant, pM), which were obtained from a binding saturation and derived from three independent experiments. 3087 AYPQKFNNNFMS(16/20) DLLAMHWNTSRQ(1/20) IQAATVPHVTES(1/20) KVKHPSSWAYYA(1/20) SNSIDKVNRPIN(1/20) 5 Phage display (common panning) 4 PMID:27133793 TiO2 nanoparticles Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 3088 QPTKDSSPPLRV(5)[0.338176 ± 0.002] STTSPPAVPHNN(1)[0.3243] PMPQYKLVVVGS(1)[0.35764] KAPTKETVWPSR(1)[0.3513] 4 Phage display (common panning) 3 PMID:27650372 The LMP1 C-terminus region Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA Activities of phages to the LMP1 C-terminus region were measured by phage ELISA. The OD values at 410 nm were measured and data shown were reproduced from the Fig 3 in the reference. 3089 TLWTDTS GLWTNVD GLSTFDV TAFTWNQ 4 Phage display (common panning) 3 PMID:27711976 Pentaerythritol trinitrate hemisuccinate(PETNH) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) 3090 LPGRTCREYPDLWWVRCY 1 Phage display (common panning) 5 PMID:27717820 The FGFR1c/KLB complex Fibroblast growth factor 21, FGF-21 Not determined. Not determined. X5CX10CX T7 phage display library (X5CX10CX) 3091 ITPAHMD(1) WDSSY@V(1) SQHTHRH(1) SGSSDQG(1) 4 Phage display (common panning) 1 PMID:27720899 Tumor necrosis factor-α(TNF-α) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Symbol @ denotes an amber stop codon. 3092 AHQQHLR(3) ATPIHWR(2) HLSHQPG(1) NISFQSS(1) 4 Phage display (common panning) 2 PMID:27720899 Tumor necrosis factor-α(TNF-α) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) 3093 HAIYPRH(11)[0.51] NLMSRPI(10)[1.47] AHQQHLR(3)[NT] ATPIHWR(2)[NT] STAPRPY(1)[NT] QFPSFTQ(1)[NT] 6 Phage display (common panning) 3 PMID:27720899 Tumor necrosis factor-α(TNF-α) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA The absorbance was measured at 450 nm using ELISA reader. In order to calculate the binding constant (Kd), the data were analyzed using Prism program (version 6.01, Graphpad Software Inc.) The specific phage with the sequences of NLMSRPI (P51) and HAIYPRH (P52) have ability to specifically bind to TNF-α with Kd of 1.47 and 0.51 nM, respectively. The irrelevant phage has no significant binding affinity towards TNF-α. In addition, the MTT assay was carried out to assess the ability of the selected P51 and P52 peptides to inhibit TNF-αcytotoxicity on L929 cells either as the peptides displayed by the phage particles or the synthesized heptamer peptides. The results of MTT assay showed that P51 and P52 peptides inhibit TNF-α cytotoxicity with IC50 values of 25.15 ± 2.18 and 7.08 ± 2.24μM, respectively. 3094 NLMSRPI(10)[1.47] IHKPQPN(4)[NT] NMMSVRG(1)[NT] LSNMHSQ(1)[NT] 4 Phage display (common panning) 4 PMID:27720899 Tumor necrosis factor-α(TNF-α) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA The absorbance was measured at 450 nm using ELISA reader. In order to calculate the binding constant (Kd), the data were analyzed using Prism program (version 6.01, Graphpad Software Inc.) The specific phage with the sequence of NLMSRPI (P51) have ability to specifically bind to TNF-α with Kd of 1.47 nM. The irrelevant phage has no significant binding affinity towards TNF-α. In addition, the MTT assay was carried out to assess the ability of the selected P51 peptide to inhibit TNF-αcytotoxicity on L929 cells either as the peptides displayed by the phage particles or the synthesized heptamer peptides. The results of MTT assay showed that P51 peptide inhibit TNF-α cytotoxicity with IC50 values of 25.15 ± 2.18 μM. 3095 HAIYPRH(11)[0.51] NLMSRPI(10)[1.47] 2 Phage display (common panning) 5 PMID:27720899 Tumor necrosis factor-α(TNF-α) Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA The absorbance was measured at 450 nm using ELISA reader. In order to calculate the binding constant (Kd), the data were analyzed using Prism program (version 6.01, Graphpad Software Inc.) The specific phage with the sequences of NLMSRPI (P51) and HAIYPRH (P52) have ability to specifically bind to TNF-α with Kd of 1.47 and 0.51 nM, respectively. The irrelevant phage has no significant binding affinity towards TNF-α. In addition, the MTT assay was carried out to assess the ability of the selected P51 and P52 peptides to inhibit TNF-αcytotoxicity on L929 cells either as the peptides displayed by the phage particles or the synthesized heptamer peptides. The results of MTT assay showed that P51 and P52 peptides inhibit TNF-α cytotoxicity with IC50 values of 25.15 ± 2.18 and 7.08 ± 2.24μM, respectively. 3096 CNTGSPYEC CQNPNQKFC CLKLGEKWC 3 Phage display (common panning) 3 PMID:27735110 The heteroternary complex with methyl viologen and cucurbit[8]uril(MV·CB[8]) Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) From the selected motifs, an epitope consisting of three amino acids (QKF) was extrapolated and incorporated into a solvent-exposed loop of a protein domain; the protein exhibited micromolar binding affinity for the MV·CB[8] complex, matching that of the cyclic peptide. By achieving selective CB[8]-mediated of a small molecule to a recombinant protein scaffold we pave the way to biomedical applications of this simple ternary system. 3097 FPWYKWRLPDVS(3) GASWLGSQWNGT(1) HLAGVSMDVSTT(1) FAETHRGFHFSF(1) HTSSLWHLFRST(1) NLLASIGPTMRI(1) MPRANASGEPHT(1) DQFVHDVKGTKH(1) 8 Phage display (common panning) 4 PMID:27371890 The acid–alkali treated titanium Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 3098 IGNSNTL(18)[0.887±0.037] LKLGEKW(4)[0.864±0.018] LPWQIHN(4)[0.649±0.014] CGNSNTL(4)[0.723±0.025] NTGSPYE(2)[0.425±0.037] NMQITKG(2)[0.335±0.016] PTVLQLT(1)[0.684±0.007] STEHTRS(1)[0.501±0.009] PTNQHHL(1)[NT] VKSTQYT(1)[0.760±0.012] MPVGAFK(1)[NT] DELHKAR(1)[0.637±0.021] ELGTVQS(1)[0.356±0.009] FGAFTPH(1)[NT] FHELTSK(1)[0.434±0.035] 15 Phage display (common panning) 4 PMID:27749918 The fifth fragment of plasminogen Plasmin light chain B Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA Affinities of the selected phage clones to Kringle 5 were measured by phage ELISA. The A410 values were measured and data shown were reproduced from the Fig. 2 in the reference. 3099 PWWWGRNV(6) NLWGFWFP(2) ESPLSLVA(1) WWGIWMQE(1) 4 Phage display (common panning) 2 PMID:27756316 Coxsackievirus A9, CAV9 Not determined. Not determined. Not determined. CX8C phage display library 3100 LWWQIWDG(4) PWWWGRNV(3) WIWAWRSS(1) LSWWSRKW(1) WWAIWMQE(1) 5 Phage display (common panning) 2 PMID:27756316 Coxsackievirus A9 lacking the RGD motif (CV-A9-RGDdel) Not determined. Not determined. Not determined. CX8C phage display library