1751 GWRLLGFGPASSFSM TRLFRVPVLPSGVTS PFARAPVEHHDVVGL [AVLIFYW](2)-R-x-P-V-x(4)-V 3 Phage display (common panning) 4 PMID:12381731 Apical membrane antigen 1, AMA1 Not determined. Not determined. Not determined. f3-15mer phage display library (X15) ELISA Phage clones displaying each of the three peptides bound to PfAMA1 in a dose-dependent manner, although the F1 (GWRLLGFGPASSFSM) and F3 (PFARAPVEHHDVVGL) peptides appeared to have an ~10-fold higher relative affinity compared with the F2 peptide (TRLFRVPVLPSGVTS). Absolute affinities were difficult to estimate from these data because the presence of up to five copies of peptide on each phage particle may impart avidity effects that are difficult to predict. Phage containing a peptide picked at random from the unpanned library and consisting of the sequence GDVWLFKTSTSHFAR (F5 peptide) were unable to bind to PfAMA1 even at phage concentrations of e11 colony-forming units/ml. Panning were performed on E. coli cell-expressed and refolded AMA1 from the 3D7 strain of P. falciparum. Three peptides with affinity for AMA1 were isolated, and characterization of their fine binding specificities indicated that they bind to a similar region on the surface of AMA1. Peptide GWRLLGFGPASSFSM was found to be a potent inhibitor of the invasion of P. falciparum merozoites into human erythrocytes. We propose that this peptide blocks interaction between AMA1 and a ligand on the erythrocyte surface that is involved in a critical step in malarial invasion. 1752 CFPWGNTWC CFPWGKEYC CFPWGNQWC CFPWGDQWC CFPWPLWAC CFPWGNEPC CFPWGDQCC CFPWGQTAC CFPWGDWPC FPWG 9 Phage display (common panning) 3 PMID:12951030 RNA-directed RNA polymerase NS5B Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Surface plasmon resonance (SPR) Peptides CFPWGKEYC, CFPWGNTWC, and CFPWGNQWC bound with varying affinities (Kd ranging from 33 to 56 μM) to the enzyme NS5B with a stoichiometry consistent with a 1:1 binding event. Surface plasmon resonance studies showed that three highly purified synthetic constrained peptides bound to immobilized NS5B with estimated Kd values ranging from 30 to 60 μM. In addition, these peptides inhibited the NS5B activity in vitro with IC 50 ranging from 6 to 48 μM, whereas in contrast they had no inhibitory effect on the enzymatic activities of calf thymus polymerase α, human polymerase β, RSV polymerase, and HIV reverse transcriptase in vitro. 1753 TWFNPFGYYSWA(5)[0.49] TWFWPYPYPHLP(3)[0.53] ENGLHNRSLNPR(3)[0.05] TLWPWAWRHNWQ(2)[0.43] TWWTGTYPWYPR(2)[0.48] TFWWHPNYYVDW(1)[0.15] GQPSHDPVPPTT(1)[0.05] SSTSTVTPAHST(1)[0.06] SSPLAHYLNAPT(1)[0.08] 9 Phage display (common panning) 3 PMID:14614029 Regulatory protein E2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA In phage ELISA, the HPV16 E2 protein was added to each well followed by addition of BSA blocking protein. BSA is immobilized separately in the absence of the E2 protein in the 96-well plate. The absorbance value (A) was determined by subtraction of the absorbance of BSA from the absorbance of the HPV16 E2. The raw A value of BSA was ~0.05 or 0.1. Among the isolated phage clones, authors found that tryptophan-rich peptide sequences appeared repetitively in successive cycles of phage library panning. Replacement of the tryptophan amino acids in these dodecapeptides reduced the degree to which these peptides bound to the E2 protein. These E2-binding peptides were tested for their ability to inhibit the transcriptional regulatory function of E2 in a test cell line, which contained an E2 gene and a luciferase reporter gene driven by an E2-dependent transcriptional promoter. 1754 CTGDARHRC(5) CNSVGRIWC(3) CTPATLLLC(2) CMRLGSSIC(2) CLVSFGLSC(2) CLDSSRGIC(2) CRQLGKQRC(1) CHQLGKQRC(1) CGGVHFAYC(1) CADVSQPVC(1) CAGFEKIPC(1) CNRLPRELC(1) CVLESHYEC(1) 13 Phage display (common panning) 4 PMID:15700752 Human antibodies eluted from the surface of infected red blood cell (iRBC) Not determined. Not determined. Not determined. fUSE5-based CX7C phage display library Of 23 randomly chosen clones that were sequenced, 13 individual sequences were detected at varying frequencies and 3 of the 13 sequences had homology with membrane proteins known to exist on iRBC. The majority of phage clones (7 out of 8 clones) selected after the 4th panning bound selectively to IgG in IHS. Specific binding of the selected phage to IgG in IHS was also confirmed using 24 IHS and 11 sera from uninfected individuals. One phage clone was the most frequently found in the sequenced clones after the 4th panning, and the binding of this clone to IgG in all IHS was greater than in any serum from uninfected individuals. 1755 CQSLPTHNC CSSQNGRIC CRTLPPILC CHLLLPRPC CQAMHNRFC CTPTVTRSC CTESTINTC CQYNPLPYC CNHTRNMAC CPSRLSSQC CTKYWARNC CHPTGLHQC CLTDRHRTC CTPSLPWLC CQGPVKPLC CDATSAQVC CKPTHYNSC CRHNNLHHC CEWTESMMC CSTNPPTQC CVNSPPTMC CTNPATPFC CLWPTLKGC CHTKIFPNC CHARNSTQC CSLTNTLLC CNPYNTSMC CNGVIHNQC CYHPSFNTC CSGSETKVC CYETKTHSC CTNRHAAGC CNLLRQQTC CVSGQESIC CLALNMSYC COPHTLPTC CNTKNFHSC CNPMKPLMC CPRSGTAYC CSTPELTFC CMTSHPTLC CPLGKLPWC CQSASPRLC CLTSPTSTC CNTSSTPHC CTQKNIAAC CTNSTLQSC CKPDAISVC CNQSTLLTC CHSPLTSSC CFPTTSRGC CGFSNFRSC CQSQNHNTC CQSIRGPMC CPSTGYSYC CPPGKSSMC CHNLKRPTC CLFNHPKYC CYSLLPRVC CTMLLFHRC CRNTDTALC CPPPQGQTC CIHAPHTQC CPGHIHRTC CLALRHSNC CSPQLAPFC CQLPAERWC CRSLTDNQC CLHKPWSRC CPFVKTQLC 70 Phage display (competitive panning) 6 PMID:15919886 Integrin alpha-V-beta-3, integrin αvβ3 Abciximab Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Abciximab was employed to elute phage from the plate-bound ??? Authors found that 11 peptides reduced the number of foci to a greater extent than did 80 μg/ml ReoPro when preincubated with Vero E6 cells. In addition, 8 of the 70 peptides had sequence similarity to SNV glycoproteins. Authors compared all 18 peptide sequences (10 most potent, 7 peptides with sequence similarity to hantavirus glycoproteins, and 1 peptide that was in the group that displayed the greatest potency and had significant sequence similarity) for their abilities to inhibit SNV, Hantaan virus (HTNV), and Prospect Hill virus (PHV) infection. There was a marked trend for the peptides to inhibit SNV and HTNV to a greater extent than they inhibited PHV, a finding that supports the contention that SNV and HTNV use β3 integrins and PHV uses a different receptor, β1 integrin. 1756 CETGAKPHC(0.2) CNPHPQQPC(0.2) CNPPPPQPC(0.2) CHPPHPQPC(0.2) CQHGAMGLC(0.2) 5 Phage display (common panning) 1 PMID:16087122 Large envelope protein Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Saturation equilibrium assay Results of equilibrium binding assay show that the concentration of the free phage clone CETGAKPHC reduces progressively with increased concentration of HBsAg. The binding data were fitted with the equation for two binding sites and the Krel D values were 2.9±0.9 nM (KrelD1) and 0.83±0.63 mM (KrelD2). The binding site of peptide ETGAKPH was located on the immunodominant region of HBsAg. An equilibrium binding assay in solution showed that the phage binds tightly to HBsAg with a relative dissociation constant (KDrel) of 2.9+/-0.9 nM. The phage bearing this peptide has the potential to be used as a diagnostic reagent and two assays for detecting HBsAg in blood samples are described. 1757 CETGAKPHC(0.5) CQTNHMGLC(0.2) CQTKHQGRC(0.1) CQPNHMGLC(0.1) CQSKPQGLC(0.1) 5 Phage display (common panning) 2 PMID:16087122 Large envelope protein Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Saturation equilibrium assay Results of equilibrium binding assay show that the concentration of the free phage clone CETGAKPHC reduces progressively with increased concentration of HBsAg. The binding data were fitted with the equation for two binding sites and the Krel D values were 2.9±0.9 nM (KrelD1) and 0.83±0.63 mM (KrelD2). The binding site of peptide ETGAKPH was located on the immunodominant region of HBsAg. An equilibrium binding assay in solution showed that the phage binds tightly to HBsAg with a relative dissociation constant (KDrel) of 2.9+/-0.9 nM. The phage bearing this peptide has the potential to be used as a diagnostic reagent and two assays for detecting HBsAg in blood samples are described. 1758 CETGAKPHC(0.75) CQTGEKPQC(0.083) CETGEKPQC(0.083) CQAFFPNAC(0.083) 4 Phage display (common panning) 3 PMID:16087122 Large envelope protein Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Saturation equilibrium assay Results of equilibrium binding assay show that the concentration of the free phage clone CETGAKPHC reduces progressively with increased concentration of HBsAg. The binding data were fitted with the equation for two binding sites and the Krel D values were 2.9±0.9 nM (KrelD1) and 0.83±0.63 mM (KrelD2). The binding site of peptide ETGAKPH was located on the immunodominant region of HBsAg. An equilibrium binding assay in solution showed that the phage binds tightly to HBsAg with a relative dissociation constant (KDrel) of 2.9+/-0.9 nM. The phage bearing this peptide has the potential to be used as a diagnostic reagent and two assays for detecting HBsAg in blood samples are described. 1759 IRPDTPR(1)[0.764 ± 0.043, 0.167 ± 0.047] KYLNAHV(1)[0.683 ± 0.015, 0.174 ± 0.023] NKVLVPP(1)[0.756 ± 0.011, 0.244 ± 0.042] VPLQPLR(1)[0.719 ± 0.038, 0.189 ± 0.013] KNVQVPL(1)[0.500 ± 0.043, 0.133 ± 0.030] KNVHPPP(1)[0.527 ± 0.017, 0.117 ± 0.030] SHQHARL(1)[0.578 ± 0.035, 0.129 ± 0.038] KNVHVPL(1)[0.572 ± 0.026, 0.123 ± 0.017] TPHTLPP(1)[0.353 ± 0.017, 0.095 ± 0.015] SLIQASA(1)[0.917 ± 0.022, 0.595 ± 0.017] 10 Phage display (competitive panning) 3 PMID:18430373 Interferon alpha/beta receptor 2, IFN-R-2 Interferon alpha-2 2HYM,2KZ1,2LAG,3S9D,3SE3, Not determined. Ph.D.-7 phage display library (X7) ELISA WISH cells prepared in 96-well plates were incubated with selected phage clones. Phage clones binding to WISH cells were detected by phage ELISA in the absence or presence of IFNα-2b, then the absorbance at 490 nm was analyzed. Wild-type M13 phage was used as a negative control. Data, expressed as mean of 3 independent experiments ± SD, were reproduced from Figure 2 in the reference. In the absence of IFNα-2b, the absorbance of M13 phage was 0.052 ± 0.033, while in the presence of IFNα-2b its value was 0.056 ± 0.017. The data in the first column of affinity values were obtained in the absence of IFNα-2b, the data in the second column of affinity values in the presence of IFNα-2b. Biopannings were performed with WISH cells, which endogenously express type I IFN receptors on the cell surface. Phages bounding to surviving cells were eluted with IFNα-2b. ts: Sixteen positive clones were obtained after 3 rounds of functional selection. Ten clones were picked from these positive clones according to the results of phage ELISA and were sequenced. The amino acid sequences homologous to IFNα-2b were defined by residues AB loop 31-37, BC loop 68-74, C helix 93-99, CD loop 106-112, D helix 115-121, DE loop 132-138, and E helix 143-161. Two of the peptides, designated clones T3 (IRPDTPR) and T9 (KNVHPPP), aligned with the IFNAR2-binding domains (AB loop and E helix), were synthesized and designated as IR-7 and KP-7, respectively. Both KP-7 and IR-7 were found to compete with GFP/IFNα-2b for receptor binding and mimicked the antiviral activity of IFNα-2b cooperatively. 1760 TSQNIRS(1) TSYHRSA(1) 2 Phage display (common panning) 3 PMID:21193836 Envelope glycoprotein E2 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) When pep7-1 (TSQNIRS) was present, the infectivity of HCV particles in cell culture was notably decreased. This decrease was demonstrated by Western blot analysis, immunofluorescence assay, and reverse transcription PCR assay. 1761 SVSVGMKPSPRP(1) SVSVGTKPRPRP(1) SVSWGMKPSPRQ(1) 3 Phage display (common panning) 3 PMID:21193836 Envelope glycoprotein E2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Pep12-1 (SVSVGMKPSPRP) showed little inhibitory effect on HCV infection. 1762 CHRCFHFRRHPVAVF TRHRHVPRFLPLRHV 2 Phage display (common panning) 3 PMID:21154952 Interleukin-10, IL-10 Interleukin-10 receptor subunit alpha (IL-10RA) 1J7V,1Y6K, Not determined. f3-15mer phage display library (X15) Each selection was performed on the streptavidine-coated plates. Fifteen-mer peptides binding to IL-10 selected from the phage display library were synthesized and tested in a bioassay using the IL-10-sensitive MC/9 cell line to measure their IL-10 blocking activity. Peptides p9 (CHRCFHFRRHPVAVF) and p13 (TRHRHVPRFLPLRHV) inhibited human IL-10-induced proliferation. Peptide binding to IL-10 was demonstrated using surface plasmon resonance analysis. It was found that p9 and p13 bound to immobilized IL-10, as compared to a control peptide. 1763 DFRRLPGAFWQLRQP(13)[0.429, 24][0.2] GWWYKGRARPVSAVA(4)[0.398, 13][0.5] VWRLLAPPFSNRLLP(1)[0.488, 1][0.2] R-x-L-P-x(2)-F-x(3)-R-x-P 3 Phage display (common panning) 5 PMID:10456319 Ganglioside GM1 Cholera toxin B protein, CTB Not determined. Not determined. X15 fUSE5 phage display library ELISA,Quartz crystal microbalance (QCM) In phage ELISA, the absorbance at 492 nm was determined. Absorbances were reproduced from the graph when the concentration of phage was 5 nM. And the value of the control phage (displaying LGRAGQSYPSFARGL) was 0.221. Besides, in binding inhibition assay, horseradish peroxidase-conjugated CTB and synthetic peptides were incubated with the GM1 plates in a 24 well plate. The IC50 values (μM) of synthetic peptides were determined and shown. Furthermore the dissociation constants (Kd values, nM) were determined by QCM and shown. Three synthetic pentadecapeptides inhibited the binding of cholera toxin B subunit to the GM1 monolayer with an IC50 of 24, 13 and 1.0 μM, respectively. These peptides will be useful for searching functional roles of ganglioside GM1. 1764 ARLSPTMVHPNGAQP(2)[1.268 ± 0.179] GLAYSRFKVSRAIWR(2)[0.283] HRWMPHVFAVRQGAS(1)[0.319 ± 0.078] ALADSIWSSRSGPGL(1)[0.310 ± 0.136] KDFLSGLRHLHFLHS(1)[0.319 ± 0.122] TFRLPLVRAQYDSSH(1)[0.139] ARVMRQVCGGTGCGV(1)[0.270 ± 0.201] TSVNRGFLLQRASHP(1)[0.192] 8 Phage display (competitive panning) 4 PMID:20476787 Hemagglutinin, HA Sialyl Lewis(X), SLX Not determined. Not determined. X15 fUSE5 phage display library ELISA,Surface plasmon resonance (SPR) In phage ELISA, the absorbance at 492 nm was determined. Data shown were reproduced from the graph and expressed as means ± the standard deviation (n = 3). Besides, clone f1 (displaying ARLSPTMVHPNGAQP) was found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8 and 8.6 nM against H1 and H3. A docking simulation suggested that, similar to sialic acid, the peptides are recognized by the receptor-binding site in HA, which indicates that these peptides mimic the sialic acid structure. N-stearoyl peptides inhibited infections by the A/Puerto Rico/8/34 (H1N1) and A/Aichi/2/68 (H3N2) strains of influenza virus. Such HA-inhibitors are promising candidates for novel antiviral drugs. 1765 EPYGFIAFSRAAHSP(4)[0.563 ± 0.310] ARLSPTMVHPNGAQP(2)[1.268 ± 0.179] TFFQVPPRILVGSAS(1)[0.170 ± 0.201] ARLGSVLISSGPSSD(1)[0.261] GRPPDSVFRSRGWLS(1)[0.891 ± 0.280] AWRNMIRYGVDLPAF(1)[0.323 ± 0.092] 6 Phage display (competitive panning) 5 PMID:20476787 Hemagglutinin, HA 6' ganglioside GM3 Not determined. Not determined. X15 fUSE5 phage display library ELISA,Surface plasmon resonance (SPR) In phage ELISA, the absorbance at 492 nm was determined. Data shown were reproduced from the graph and expressed as means ± the standard deviation (n = 3). Besides, clones f1 (displaying ARLSPTMVHPNGAQP), f9 (displaying EPYGFIAFSRAAHSP) and f12 (displaying GRPPDSVFRSRGWLS) were found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8-30nM against H1 and H3. A docking simulation suggested that, similar to sialic acid, the peptides are recognized by the receptor-binding site in HA, which indicates that these peptides mimic the sialic acid structure. N-stearoyl peptides inhibited infections by the A/Puerto Rico/8/34 (H1N1) and A/Aichi/2/68 (H3N2) strains of influenza virus. Such HA-inhibitors are promising candidates for novel antiviral drugs. 1766 ARMRYVDLPVVSGIS(3)[0.117 ± 0.018] GRVPVFGLSPLFKVE(2)[1.132 ± 0.131] ARLSPTMVHPNGAQP(2)[1.276 ± 0.075] EPYGFIAFSRAAHSP(1)[0.716 ± 0.389] IDIAFSSLALADISR(1)[1.018 ± 0.210] 5 Phage display (competitive panning) 4 PMID:20476787 Hemagglutinin, HA Sialyl Lewis(X), SLX Not determined. Not determined. X15 fUSE5 phage display library ELISA,Surface plasmon resonance (SPR) In phage ELISA, the absorbance at 492 nm was determined. Data shown were reproduced from the graph and expressed as means ± the standard deviation (n = 3). Besides, clones f1 (displaying ARLSPTMVHPNGAQP), f9 (displaying EPYGFIAFSRAAHSP) and f12 (displaying GRPPDSVFRSRGWLS) were found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8-30nM against H1 and H3. A docking simulation suggested that, similar to sialic acid, the peptides are recognized by the receptor-binding site in HA, which indicates that these peptides mimic the sialic acid structure. N-stearoyl peptides inhibited infections by the A/Puerto Rico/8/34 (H1N1) and A/Aichi/2/68 (H3N2) strains of influenza virus. Such HA-inhibitors are promising candidates for novel antiviral drugs. 1767 ARLSPTMVHPNGAQP(9)[1.276 ± 0.075] IDIAFSSLALADISR(1)[1.018 ± 0.210] 2 Phage display (competitive panning) 5 PMID:20476787 Hemagglutinin, HA 6' ganglioside GM3 Not determined. Not determined. X15 fUSE5 phage display library ELISA,Surface plasmon resonance (SPR) In phage ELISA, the absorbance at 492 nm was determined. Data shown were reproduced from the graph and expressed as means ± the standard deviation (n = 3). Besides, clones f1 (displaying ARLSPTMVHPNGAQP) and f16 (displaying IDIAFSSLALADISR) were found to have a high affinity by SPR analysis, with dissociation constant (Kd) values of 7.8-19nM against H1 and H3. A docking simulation suggested that, similar to sialic acid, the peptides are recognized by the receptor-binding site in HA, which indicates that these peptides mimic the sialic acid structure. N-stearoyl peptides inhibited infections by the A/Puerto Rico/8/34 (H1N1) and A/Aichi/2/68 (H3N2) strains of influenza virus. Such HA-inhibitors are promising candidates for novel antiviral drugs. 1768 QLMHDYR(1)[6.7] LSQSLTR(1)[5.7] RACSKDA(1)[5.1] ANTLRSP(1)[4.8] KHVPKMH(1)[4.6] AHPALPL(1)[3.9] YLTMPTP(1)[2.7] VYLTGPS(1)[2.7] 8 Phage display (common panning) 4 PMID:18500833 α form of poly(L-lactide) crystalline films Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA,Surface plasmon resonance (SPR) The binding of all phage clones, which were identified after four rounds of biopanning against the α form of PLLA films, at a 200 pM phage concentration was analyzed by ELISA. The apparent binding constants (Kapp, 1.0e9 1/M) for films composed of the α form of PLLA were estimated and shown. The value of the library was 1.6e9 1/M. Besides, the real-time analysis of the binding of synthetic peptide (QLMHDYR) freed from the phage particles against the polymer films was performed using a BIAcore X. The binding constant (Ka) for the α form of PLLA was determined to be 6.1e4 1/M. The binding of all phage clones, which were identified after four rounds of biopanning against the R form of PLLA films, at a 200 pM phage concentration was analyzed by ELISA. Therefore, eight prospective clones that showed relatively large binding amounts for the ??? 1769 DYFSSPYYEQLF WPGWHHVPPAVS GHWHHITKVSKQ 3 Phage display (subtractive panning) 5-6 PMID:15379530 Single-walled carbon nanotubes, SWNTs Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) To minimize background binding, the phage library was pre-incubated with M-280 streptavidin-coated magnetic beads. Unbound phages were incubated with the SWNHs-magnetic bead complexes. SWNHs-magnetic bead complexes were formed by mixing the sonicated biotinylated SWNHs with streptavidin-coated magnetic beads. Authors selected 33 phage clones from panning cycle 5 and 15 phage clones from panning cycle 6 (total of 48 phage clones), and the pIII tail sequences were identified via standard DNA sequencing techniques. Among the 48 clones, a total of 28 clones (i.e., 15 out of the 33 clones from panning cycle 5 and 13 out of the 15 clones from panning cycle 6) have been shown to display an identical peptide sequence, DYFSSPYYEQLF, that is enriched in polar and aromatic residues. 1770 HSSYWYAFNNKT HTSYWYAFNTKT YTTHVKPFAPSS HAWVDWIRPIH 4 Phage display (common panning) 4 PMID:16402784 Single-walled carbon nanotubes, SWNTs Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 1771 GETRAPL(7)[0.948 ± 0.058] FPGRPSP(6)[0.902 ± 0.100] YLTMPTP(2)[0.901 ± 0.026] FSWEAFA(1)[0.976 ± 0.029] HLESTPG(1)[0.884 ± 0.034] RHEPPLA(1)[0.857 ± 0.052] GETQCAA(1)[0.836 ± 0.086] HTAQSTA(1)[0.961 ± 0.049] 8 Phage display (common panning) 4 PMID:17492699 Syndiotactic polystyrene film Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ELISA In phage ELISA, the absorbance at 405 nm was determined. Data were reproduced from the graph and shown as means ± standard deviations. The absorbance for negative control was 0.592 ± 0.007. 1772 LAYWEFVFHPQGDDL 1 Phage display (common panning) 3 PMID:7649995 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. X15 phage display library Following three rounds of enrichment and amplification, the 15-mer library was enriched for peptides containing the HPQ epitope in a sequence such as LAYWEFVFHPQGDDL. 1773 PWAWLT PWAWLI 2 Phage display (common panning) 3 PMID:7649995 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. X6 fUSE5 phage dislpay library 1774 LFYYLH(4) VFYYLH(3) RFYYLH(1) AFYYLH(1) HFYYLH(1) PPYYLH(4) PVYYLH(3) GVFYLH(2) RVWYLH(2) GPWYLH(1) QLYFLH(4) QLFFLH(2) QLYRLH(2) [YFW]-[YF]-L-H 13 Phage display (common panning) 2 PMID:7685302 Anti-biotin polyclonal antibody Biotin Not determined. Not determined. f3-6mer phage display library (X6) Each of the phage isolated in the anti-biotin antibody panning were coated on ELISA wells and their ability to bind streptavidin coupled to horseradish peroxidase evaluated. None bound above the background levels of a control phage. 1775 GDWVFI(6) GDWAFI(1) GDFRFT(1) GNFVFI(1) VDWAFI(1) PWPWLG(4) PWLWLQ(1) PWDWLY(1) AFWAWL(2) TWWGYL(1) 9 Phage display (competitive panning) 2 PMID:7685302 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. f3-6mer phage display library (X6) Only phage displaying the GDWVFI and PWPWLG peptides demonstrated biotin-sensitive streptavidin binding in ELISA and micropanning assays. Binding of streptavidin to phage displaying GDWVFI was also confirmed by a BIACORE analysis; both biotin and synthetic HPQ peptide [YGGHPQGG] blocked this binding. Phage displaying GDWVFI could be eluted from streptavidin with either acid or biotin, but not phosphate-buffered saline, whereas phage displaying PWPWLG eluted with acid, biotin and phosphate-buffered saline. The possibility that PWPWLG sticks nonspecifically to plastic was considered; however, it was found that PWPWLG did not bind well unless wells were coated with streptavidin.