826 MDDDTERFPTHRSLP[1.16] XPPFTSAVGGVDHRS[0.45] STTNTPLVSHLEHRS[0.42] LEHRS 3 Phage display (common panning) PMID:10725197 Anti-gG2 monoclonal antibody H5 Envelope glycoprotein G, gG, gG-2 Not determined. Not determined. f3-15mer phage display library (X15) ELISA In ELISA, the wild-type phage f88-4 was used as negative control. Absorbance at 490 nm was measured. Data shown were reproduced from the graph. The A490 of the wild-type phage f88-4 was 0.30. 827 QPTSKPTRPWLVSFL NAETAFSLSSFPPSP 2 Phage display (common panning) PMID:10725197 Anti-gG2 monoclonal antibody H7 Envelope glycoprotein G, gG, gG-2 Not determined. Not determined. f3-15mer phage display library (X15) 828 TPESTPLLPPFPRSV ALSSQGGMSPEPTPL DYTPQTSLELPPESF TPL 3 Phage display (common panning) PMID:10725197 Anti-gG2 monoclonal antibody F11 Envelope glycoprotein G, gG, gG-2 Not determined. Not determined. f3-15mer phage display library (X15) 829 YMQPDPPPPLHAPDY SPLPEPPPEHRALVP TSTPTEHTYPLEIIT P(3)-E-H 3 Phage display (common panning) PMID:10725197 Anti-gG2 monoclonal antibody E5 Envelope glycoprotein G, gG, gG-2 Not determined. Not determined. f3-15mer phage display library (X15) 830 GEASGLCCRWSSLKGC(30)[NA] GHREAFLPPWVFXFL(11)[NA] GEASGLCCRWSLRVV(8)[NA] YFTIPATLLPFGV(1)[NA] GNRPVRPQVYFSASS(1)[82%] SGFVAGKGFRLDFGS(1)[88%] 6 Phage display (common panning) 3 PMID:10649627 Anti-MAPS monoclonal antibody 9C10 Meningococcal group A polysaccharide (MAPS) Not determined. Not determined. f3-15mer phage display library (X15) ELISA Six phage clones were screened for MAPS mimicry by their ability to inhibit binding of human hyperimmune sera to nominal antigen, MAPS, by inhibition ELISA. The results of the inhibition ELISA with phage clone six (SGFVAGKGFRLDFGS) indicate that 5.5e10 TU of phage clone 6 inhibited the binding of human hyperimmune sera to MAPS (88% inhibition). The control phage, containing no insert, failed to inhibit binding in this assay. Phage clone 4 (GNRPVRPQVYFSASS) was also capable of inhibiting the binding of human hyperimmune sera to MAPS (82% inhibition). Other phage clone failed to inhibit binding of human hyperimmune sera to MAPS (data not shown). 831 RVVMSYPRHYWFSVR TRLGRIYWAAPSGIV ASRHAIRFIVFPAT LPLVFLTCLIMLSRV VSAAPTPAYWFGFYY 5 Phage display (common panning) PMID:10552746 Pancreatic alpha-amylase, PA Not determined. Not determined. Not determined. f3-15mer phage display library (X15) The two phage display ligands (RVVMSYPRHYWFSVR and TRLGRIYWAAPSGIV) with high-binding activities contained a high content of Arg, Tyr, and Trp residues with the short consensus sequence Arg-X-Tyr-Trp. These clones were shown to exhibit comparable binding interactions toward barley R-amylase based on transducing units titering and measurement of the dissociation constants. 832 ALSMWQPT LRWSQPTN APLTSPMM YNGRRKQV LLVRGLAP VSTVLGST KRVKSTSF HALAKRVV SRLMASSH YLVPNNN YEPVPVRG 11 Phage display (common panning) 5 PMID:11717916 Anti-c-myc protein monoclonal antibody 9E10 Myc proto-oncogene protein Not determined. Not determined. X8 phage display library The binding of peptides to 9E10 could be specifically inhibited by free c-myc decapeptide. 833 ASNHTHSSSIQF(3) EPIHRSTLTALL(1) EPIHRSTLTAPL(1) YQDMIYMRPLDS(1) DARHSSSLQMLF(1) FSLRPTMNFTNL(1) DPGKIYFHIAVS(1) PRPSPKMGVSV(1) TATHRHSSSI(1) 9 Phage display (common panning) 4 PMID:11694293 pFc' fragments of HAT Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 834 SHLGFDD(3) RQLVQPL(1) SPAPSDS(1) SSQSDPA(1) SKPTQLH(1) GTATSPH(1) TSDTGWR(1) 7 Phage display (common panning) 4 PMID:11694293 pFc' fragments of HAT Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) The constant region of humanized anti-Tac (HAT), prepared by pepsin digestion and receptor-affinity chromatography, was used as the target for phage display in this study. 835 KPGDPSALHVVRCWIC(2) DGRRDVVVRSATFYL(1) EGLYSPWWPRSLPVL(1) SSKTRSFGVHLVGPY(1) LPPGLHVFPLASNRS(1) 5 Phage display (common panning) 3 PMID:11468163 Anti-GPIb monoclonal antibody 6B4 Platelet glycoprotein Ib alpha chain Not determined. Not determined. X15 phage display library 836 KPGEMR(3) CDTLKPGEC(3) CNKPGERTC(2) CADQKPGEC(2) CYKPGEWAC(1) CKPGEVQQC(1) CKPVENRAC(1) KPGEMRGAA(1) 8 Phage display (common panning) 3 PMID:11468163 Anti-GPIb monoclonal antibody 6B4 Platelet glycoprotein Ib alpha chain Not determined. Not determined. CX7C fUSE5 phage display library 837 PVLLFCFLAGRCVSV(7) LRCYSHCTFYFASST(1) 2 Phage display (common panning) 3 PMID:11468163 Anti-GPIb monoclonal antibody 12G1 Platelet glycoprotein Ib alpha chain Not determined. Not determined. X15 phage display library 838 MCPEMSFVAVHSCAR(15) 1 Phage display (common panning) 3 PMID:11468163 Anti-GPIb monoclonal antibody 12E4 Platelet glycoprotein Ib alpha chain Not determined. Not determined. X15 phage display library 839 GFLSSCNFRFCELVR(24) 1 Phage display (common panning) 3 PMID:11468163 Anti-GPIb monoclonal antibody 27A10 Platelet glycoprotein Ib alpha chain Not determined. Not determined. X15 phage display library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hage display (common panning) 4 PMID:10064083 HLA class II histocompatibility antigen, DRB1-1 beta chain HLA class II histocompatibility antigen, DM Not determined. Not determined. M13lib phage display library ELISA Purified DR1 molecules (35 nM) were incubated with the N-terminal biotinylated peptide GFKA7 (0.2 μM) and competitor peptides in concentrations ranging from 0.001 to 100 μM. Competitive peptide binding to DR1 was analyzed using the high-throughput ELISA-based assay. IC50 (μM) values represent the concentration of peptide competitors yielding 50 % binding inhibition of biotinylated GFKA7 to DR1. 841 GPRPPSP(1) GPRPTGH(1) GPRPHTP(1) GPRPPAP(1) GPRPPSH(1) GPRPPMS(1) GPRPHLM(1) GPRPNLT(1) GPRPPYA(1) GPRPATM(1) GPRPVNP(1) LHSTTFW(1) KHATTFW(1) EHSLTFW(1) DHVNTFW(1) ATPIRQP(1) ASTSESL(1) GPRP 17 Phage display (common panning) 1 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A series of peptides containing the Gly-Pro-Arg-Pro motif efficiently blocked the binding of phage having the same motif, presumably by binding to their common target. 842 HLHGTPRPSSGL(12) HLHGTPRMLPPL(3) GPRPPLPPALPL(2) GPRPPVAGSWPF(2) GPRPWPPQELSR(1) GPRPPAALPHPL(1) GPRPPSLPPDPA(1) GPRPSMGLATNL(1) GPRPLNPPDKLP(1) GPRPVYPRHDYT(1) GPRPPSATAFPP(1) GPRPAHPPPLTH(1) GPRPPASNFSFG(1) GPRPHTILTSPS(1) GPRPATTWYPNS(1) GPRPSLSHAHNW(1) GPRPAWTSPTFI(1) GPRPPSTHWMQQ(1) GPRPNFPSLPTQ(1) GPRPNPLTVALH(1) GPRPPITMPMFM(1) GPRPVHNTFYYA(1) GPRPATYMPPSL(1) GPRPLYTLSPHT(1) LLAGPRPPSMHV(1) GPRP 25 Phage display (common panning) 1 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A series of peptides containing the Gly-Pro-Arg-Pro motif efficiently blocked the binding of phage having the same motif, presumably by binding to their common target. 843 CAGPRPNPS(13) CAGPRPALG(6) CAGPRPPHC(1) CKTNDNTQC(1) CQGDPSHHC(1) CLNTSSMTC(1) CSTAVGPQC(1) CELSARGMC(1) CNHQHNNAC(1) CKSGLTPTC(1) CRVNFQNVC(1) GPRP 11 Phage display (common panning) 1 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A series of peptides containing the Gly-Pro-Arg-Pro motif efficiently blocked the binding of phage having the same motif, presumably by binding to their common target. 844 GHWKWYE(1) SHYMRMQ(1) NHYMSWQ(1) NHYTPLW(1) THMIEFW(1) SHFQNFW(1) SHYRNPQ(1) SHYTQFY(1) HHYTLPQ(1) SHYPYWE(1) HHADGDT(1) NHHAMFW(1) SHY 12 Phage display (common panning) 2 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A second round of panning was performed against the same target mixture in the presence of this blocking peptide. Phage recovered from this second panning exhibited a motif (Ser-His-Tyr) that was subsequently shown to bind specifically to complement component C1q. A second peptide containing this motif specifically blocked the interaction of the phage with C1q. 845 FHWSWYTPSRPS(2) NHMSRWEAWDRL(2) HLHGTPRMLPPL(2) HLHGTPRPSSGL(2) AHLRQDSAWKLN(1) SHTPDRPGAFYA(1) SHYTSTWAASEG(1) SHYPQELWAGSS(1) SHY 8 Phage display (common panning) 2 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A second round of panning was performed against the same target mixture in the presence of this blocking peptide. Phage recovered from this second panning exhibited a motif (Ser-His-Tyr) that was subsequently shown to bind specifically to complement component C1q. A second peptide containing this motif specifically blocked the interaction of the phage with C1q. 846 CAHHLKQFW(1) CAAHYGYEW(1) CWFAPHLSC(1) CWFAPHLRC(1) 4 Phage display (common panning) 2 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A second round of panning was performed against the same target mixture in the presence of this blocking peptide. Phage recovered from this second panning exhibited a motif (Ser-His-Tyr) that was subsequently shown to bind specifically to complement component C1q. A second peptide containing this motif specifically blocked the interaction of the phage with C1q. 847 FNPFLLD(9) YWNPFFL(4) FNPFSAG(1) SYALRAP(1) ALGLSPL(1) KVWIPQK(1) NPL 6 Phage display (common panning) 3 PMID:10677284 High molecular mass serum fraction Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Here this procedure is used to probe a mixture of high molecular mass components of human cord blood with phage-peptide display libraries. The initial panning recovered phage that bore the consensus motif Gly-Pro-Arg-Pro, a known fibrinogen-binding motif. These phage bound specifically to purified fibrinogen. A second round of panning was performed against the same target mixture in the presence of this blocking peptide. Phage recovered from this second panning exhibited a motif (Ser-His-Tyr) that was subsequently shown to bind specifically to complement component C1q. A third round of panning performed in the presence of both the fibrinogen- and the C1q- blocking peptides yielded phage with a new peptide motif (Asn-Pro-Phe) that also bound specifically to C1q, apparently at a new site. 848 CRYRGDLGRRC(8) 1 Phage display (common panning) 4 PMID:11006114 Madin-Darby canine kidney cells strain II, MDCKII Not determined. Not determined. Not determined. pVIII-9aa.Cys phage display library (CX9C) MDCK strain II (MDCKII) cells transfected with a rabbit receptor for polymeric immunoglobulins (pIgR) were kindly provided by Dr. K. E. Mostov (University of California). The identified peptide contained a putative integrinbinding (RGD) motif suggesting the involvement of integrins, but not pIgR, in phage transcytosis. The paper data suggest the feasibility of using short peptides for targeting transcytotic pathways nand facilitating delivery of macromolecules across cellular barriers. 849 SVSVGMKPSPRP(16) 1 Phage display (competitive panning) 5 PMID:10856231 Tobacco plasmodesmal-enriched cell wall fraction, W2 cell fraction Homeotic protein knotted-1 Not determined. Not determined. Ph.D.-12 phage display library (X12) Elution of bound phages was achieved by addition of KN1. A KN1 peptide antagonist had the capacity to interact with a motif involved in the dilation of plasmodesmal microchannels. 850 QDVHLTQQSRYT(7) SFHLELLERGQS(6) LSTHTTESRSMV(1) DPLNKMLLSQDL(1) 4 Phage display (competitive panning) 5 PMID:10856231 Tobacco plasmodesmal-enriched cell wall fraction, W2 cell fraction Movement protein, MP Not determined. Not determined. Ph.D.-12 phage display library (X12) Elution of bound phages was achieved by addition of CMV-MP.