551 SVSVGMKPSPRP(0.4) VGISKPWAGPSV(0.2) SYTNQIYRQNHP(0.2) YVYVGMKPSPRP(0.2) 4 Phage display (common panning) 4 PMID:19634182 Semiconductor crystalline surface CdSe(100) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 552 SVSVGMKPSPRP(1.0) 1 Phage display (common panning) 6 PMID:19634182 Semiconductor crystalline surface CdSe(100) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 553 CDQRTTRLC(1) CPHDPNHPC(1) CQSQTRNHC(1) CLQDMRQFC(1) CLPTDPIQC(1) CPDHPFLRC(1) CSTRAENQC(1) CPSHLDAFC(1) CKTGHMRIC(1) CVRTPTHHC(1) CSGVINTTC(1) CPLASTRTC(1) CSQFPPRLC(1) CLLNKQNAC(1) CKFPLNAAC(1) CSLTPHRSC(1) CKPWPMYSC(1) CLQHDALNC(1) CNANKPKMC(1) CPKHVLKVC(1) CTPDKKSFC(1) CHGKAALAC(1) CNLMGNPHC(1) CLKNWFQPC(1) CKEYGRQMC(1) CQPSDPHLC(1) CSHLPPNRC(1) 27 Phage display (competitive panning) PMID:19515773 Glycoprotein Gn, glycoprotein G1 Anti-glycoprotein G1 monoclonal antibody 6B9/F5 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G1 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G1. The glycoprotein G1 locates at 4-545 of the glycoprotein precursor (GI:30313865). The in vitro ANDV infection inhibition rate of phages bearing these peptides were lower than 30%. 554 CSPLLRTVC(1) CHKGHTWNC(1) CINASHAHC(1) CWPPSSRTC(1) CPSSPFNHC(1) CEHLSHAAC(1) CQDRKTSQC(1) CTDVYRPTC(1) CGEKSAQLC(1) CSAAERLNC(1) CFRTLEHLC(1) CEKLHTASC(1) CSLHSHKGC(1) CNSHSPVHC(1) CMQSAAAHC(1) CPAASHPRC(1) CKSLGSSQC(1) 17 Phage display (competitive panning) PMID:19515773 Glycoprotein Gn, glycoprotein G1 Anti-glycoprotein G1 monoclonal antibody 6B9/F5 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G1 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G1. The glycoprotein G1 locates at 4-545 of the glycoprotein precursor (GI:30313865). The in vitro ANDV infection inhibition rate of phages bearing these peptides were between 30% and 60%. 555 CPSNVNNIC(1) 1 Phage display (competitive panning) PMID:19515773 Glycoprotein Gn, glycoprotein G1 Anti-glycoprotein G1 monoclonal antibody 6B9/F5 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G1 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G1. The glycoprotein G1 locates at 4-545 of the glycoprotein precursor (GI:30313865). The phage bearing peptide CPSNVNNIC is the most potent phage identified by elution with the anti-Gn antibody 6B9/F5. It inhibited hantavirus entry by greater than 60%. 556 CTTMTRMTC(2) CHPGSSSRC(1) CSLSPLGRC(1) CTARYTQHC(1) CHGVYALHC(1) CLQHNEREC(1) CHPSTHRYC(1) CPGNWWSTC(1) CGMLNWNRC(1) CPHTQFWQC(1) CTPTMHNHC(1) CDQVAGYSC(1) CIPMMTEFC(1) CERPYSRLC(1) CPSLHTREC(1) CSPLQIPYC(1) 16 Phage display (competitive panning) PMID:19515773 Glycoprotein Gc, glycoprotein G2 Anti-glycoprotein G2 monoclonal antibody 6C5/D12 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G2 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G2. The glycoprotein G2 locates at 653-1137 of the glycoprotein precursor (GI:30313865). The in vitro ANDV infection inhibition rate of phages bearing these peptides were lower than 30%. 557 CNKPFSLPC(1) CHNLESGTC(1) CNSVPPYQC(1) CSDSWLPRC(1) CSAPFTKSC(1) CEGLPNIDC(1) CTSTHTKTC(1) CLSIHSSVC(1) CPWSTQYAC(1) CTGSNLPIC(1) CSLAPANTC(1) CGLKTNPAC(1) CRDTTPWWC(1) CHTNASPHC(1) CTSMAYHHC(1) CSLSSPRIC(1) CVSLEHQNC(1) CRVTQTHTC(1) CPTTKSNVC(1) CSPGPHRVC(1) CKSTSNVYC(1) CTVGPTRSC(1) 22 Phage display (competitive panning) PMID:19515773 Glycoprotein Gc, glycoprotein G2 Anti-glycoprotein G2 monoclonal antibody 6C5/D12 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G2 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G2. The glycoprotein G2 locates at 653-1137 of the glycoprotein precursor (GI:30313865). The in vitro ANDV infection inhibition rate of phages bearing these peptides were between 30% and 60%. 558 CPMSQNPTC(1) CPKLHPGGC(1) 2 Phage display (competitive panning) PMID:19515773 Glycoprotein Gc, glycoprotein G2 Anti-glycoprotein G2 monoclonal antibody 6C5/D12 Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) In fact, density gradient-purified, UV-treated Andes Virus (ANDV) strain CHI-7913 was used in panning. However, glycoprotein G2 is regarded as the target since the peptides were eluted with a monoclonal antibody against the glycoprotein G2. The glycoprotein G2 locates at 653-1137 of the glycoprotein precursor (GI:30313865). From phages eluted with the anti-Gc antibody 6C5/D12, those bearing peptide CPMSQNPTC and CPKLHPGGC inhibited hantavirus entry by 66% and 72%, respectively. 559 HSIRNDVRLPSM(7) HSIRTQWTQTQV(4) HSIRQYFTLPAP(3) TNRHNPHHLHHV(3) TPHLQSGFLLTL(3) HISR 5 Phage display (common panning) 3 PMID:19493004 S-ribosylhomocysteine lyase Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) TNRHNPHHLHHV was shown to partially inhibit the activity of the LuxS enzyme. Furthermore, 14 peptides containing the consensus sequence HSIR showed high affinity with LuxS. 560 SAMWDF(3)[2.4 ± 0.13, 1.82 ± 0.09] SFIWDF(2)[2.1 ± 0.15, 1.70 ± 0.10] TNMWDF(2)[2.05 ± 0.12, 1.42 ± 0.08] ITMWDF(2)[2.2 ± 0.13, 1.36 ± 0.06] SDWWDF(1)[2.1 ± 0.10, 1.48 ± 0.12] [ST]-x(2)-W-D-F 5 Phage display (common panning) 3 PMID:19118103 Anti-hCXCR1 monoclonal antibody 5A12 C-X-C chemokine receptor type 1, CXC-R1, CXCR-1 Not determined. Not determined. fdMED1-based X6 phage display library ELISA ELISA was used to test the reactivity of mAb 5A12 with phage-peptide clones and the corresponding synthesized peptides, respectively. For phage ELISA, the absorbance was measured at 450 nm (A450 nm). Data shown are A450nm after substraction of background. For peptide ELISA, the absorbance was measured at 450 nm (A450 nm). As control, the linear hexapeptide MRFIAW was used. Data shown were reproduced from the graph. The A450 of MRFIAW is 0.06. The phage bearing the peptides showed specific binding to immobilized mAb 5A12. In FACScan analysis, all selected phage peptides were able to strongly inhibit the binding of mAb 5A12 to hCXCR1-transfected preB 300-19 murine cells. Furthermore, synthetic peptides of the corresponding phage epitopes were effective in blocking the antibody-CXCR1 interactions and to inhibit the binding of hCXCL8 to hCXCR1 transfectants. In vivo, SAMWDF blockade hCXCL8-induced neutrophil recruitment in skin inflammation in rabbits. 561 FWDDFW(4)[2.3 ± 0.15, 1.90 ± 0.15] LWDDFW(2)[1.73 ± 0.12, 1.60 ±0.16] MWNDFW(2)[1.91 ± 0.10, 1.79 ± 0.15] FWLDFW(2)[1.89 ± 0.09, 1.61 ± 0.11] [FLM]-W-x-D-F-W 4 Phage display (common panning) 3 PMID:19118103 Anti-hCXCR2 monoclonal antibody 6C6 C-X-C chemokine receptor type 2, CXC-R2, CXCR-2 Not determined. Not determined. fdMED1-based X6 phage display library ELISA ELISA was used to test the reactivity of mAb 6C6 with phage-peptide clones and the corresponding synthesized peptides, respectively. For phage ELISA, the absorbance was measured at 450 nm (A450 nm). Data shown are A450nm after substraction of background. For peptide ELISA, the absorbance was measured at 450 nm (A450 nm). As control, the linear hexapeptide MRFIAW was used. Data shown were reproduced from the graph. The A450 of MRFIAW is 0.05. The phage bearing the peptides showed specific binding to immobilized mAb 6C6. In FACScan analysis, all selected phage peptides were able to strongly inhibit the binding of mAb 6C6 to hCXCR2-transfected preB 300-19 murine cells. Furthermore, synthetic peptides of the corresponding phage epitopes were effective in blocking the antibody-CXCR2 interactions and to inhibit the binding of hCXCL8 to hCXCR2 transfectants. In vivo, FWDDFW blockade hCXCL8-induced neutrophil recruitment in skin inflammation in rabbits. 562 YTTPPYYVWEWM(1)[1.68] YSPSWDYLTFLM(1)[1.84] YTGQGWQLILPM(1)[0.38] YSEPVSFGWLWM(1)[1.75] YSDMPSDWLFPM(1)[1.84] YGEDANSWFVFM(1)[1.98] YENELGEWWLFM(1)[1.92] YTAPPWNWEWAM(1)[1.94] YQPSSALSSWMM(1)[1.74] YSDTDWMYFSTM(1)[2.05] 10 Phage display (common panning) 5 PMID:19228693 Platelet glycoprotein VI, GPVI Not determined. Not determined. Not determined. Y-X10-M phage display library ELISA Optical density at 450 nm was measured. Data were reproduced from the graph. The human GPVI protein (residues Gln21-Phe234) was expressed as a chimera with a human IgG Fc2 portion at the C terminus using the pcDNA3.1 vector expressed by CHO cells was used as the target. Platelet glycoprotein VI (GPVI) is a major collagen receptor on the platelet surface that recognizes the glycine-proline-hydroxyproline (GPO) sequence in the collagen molecule and plays a crucial role in thrombus formation. These 10 clones were examined for their GPVI-binding ability in phage enzyme-linked immunosorbent assay. A recombinant protein irrelevant to GPVI, which has human IgG-Fc, was used as a control protein. The phage bearing YTGQGWQLILPM bind neithor GPVI-Fc2 nor the control protein. The other nineclones bound to GPVI-Fc2 and did not bind to the control protein. 563 ATWVSPY(6) AHSMGTG(1) FSSQMRY(1) GVGLPHT(1) QIEPLAL(1) RIVLPTY(1) VQQVALL(1) IVLPVPY(1) GHWTRLA(1) NLPLHST(1) 10 Phage display (common panning) 3 PMID:20091097 Commercially pure titanium, cp-Ti Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ATWVSPY exhibited the strongest binding affinity to cp-Ti disks. 564 ATWVSPY(8) GVGLPHT(2) 2 Phage display (common panning) 4 PMID:20091097 Commercially pure titanium, cp-Ti Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) ATWVSPY exhibited the strongest binding affinity to cp-Ti disks. 565 QTPLTMAALELF(23) DTPLTTAALRLV(17) ETQLTTAGLRLL(9) ETPLTETALKWH(8) QTPLTETALKWH(4) QTPLTMAALELL(2) HLQDGSPPSSPH(2) GHVTTLSLLSLR(2) ETPLTEPAFKRH(2) T-x-L-T-x(3)-L 9 Phage display (common panning) 3 PMID:18973474 Anti-H5N1 virus monoclonal antibody 8H5 Hemagglutinin Not determined. Not determined. Ph.D.-12 phage display library (X12) A total of 190 randomly picked clones of screened phage were individually tested by ELISA for 8H5 binding. Among them, 69 reactive clones were sequenced. 566 CNDFRSKTC(0.47)[0.87 ± 0.02] CQHSTKWFC(0.105)[2.29 ± 0.05] CLPYAAKHC(0.05)[1.09 ± 0.04] CILGDKVGC(0.05)[1.16 ± 0.06] 4 Phage display (common panning) 4 PMID:19497129 Avian influenza virus (H9N2) particles Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) ELISA Optical density at 410 nm was measured. Data were reproduced from the graph. After the 4th round, 35 individual clones were sequenced. However, only the sequences above were given in the original paper. Among them, the phage displaying the peptide NDFRSKT possessed good anti-viral properties in vitro and in ovo. This peptide inhibited the hemagglutination activity of the viruses but showed very little and no effect on neuraminidase and hemolytic activities respectively. The phage-antibody competition assay proved that this peptide competed with anti-influenza H9N2 antibodies for the binding sites. Based on yeast two-hybrid assay, we observed that NDFRSKT inhibited the viral replication by interacting with the HA protein and this observation was further confirmed by coimmunoprecipitation. 567 CHPQFLSLC(0.55) CGLYNHPQC(0.27) 2 Phage display (common panning) 3 PMID:19497129 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) Twenty clones were sequenced from the 3rd round of panning against Streptavidin. However, only the sequences above were given in the original paper. 568 HYKWLNDPLAAW(1) 1 Phage display (common panning) 4 PMID:19349218 Anti-cEG95 polyclonal antibody EG95 host-protective vaccine antigen Not determined. Not determined. Ph.D.-12 phage display library (X12) Twelve phage clones from the 20 mer library, and eight from the 12 mer library were selected and shown to present different peptides. However, only the peptide E100, i.e. HYKWLNDPLAAWone was given in the original paper. 569 FLLEPHLMDTSM(47) FLLEPHTVTWGA(16) FLIEPWHSSLQS(11) AFLFSPLLAWPT(6) TYRFGPLEPVAF(2) F-L-[LI]-E-P 5 Phage display (subtractive panning) 4 PMID:18563328 Hepatocellular carcinoma cell line HepG2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) In the process of the second round of panning, the amplified phages were incubated with human liver cell line L02 cells at first to remove phages binding to human liver cells. Among 100 phages that specifically bound to and internalized in HepG2 cells, 82 clones demonstrated highly specific affinity to HepG2 cells and their binding to L02 cells was relatively weak. 570 FKFWLYEHVIRG(6) YWFHNFPTKMYA(4) FYRFVGDHKQLY(4) YIWPLMGSHYAK(2) WHYGVELWIRRF(1) 5 Phage display (common panning) 3 PMID:19056299 96-well immunoassay plate (polystyrene, PS) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) FKFWLYEHVIRG-fused proteins showed a considerably improved affinity to polystyrene microplate, indicating its application in diagnostic technology such as enzyme-linked immunosorbent assay (ELISA). 571 NSLSNHFRSQHS NNINQFFRSQPF TTLNSFMRSFPP HANLNGWLRTLS SLNNWFRLTPAP HKSPNSLNDFLR ELNTFFRWTTGG TDLNTFLRSLTS NPHLNHIFRSKM IPTLNQHVRASG TLNQWFRPLPTS TLNDFFHNPPHP SLNEHFRPIKQF LITFFRWTTPLK RQNNSLSMFFAG SLNQFFMTSSPA LNQWFRPSPTSG ANSLDNWFRIFP NLNQHIRSLSIP MNLGMDDPRMRR HLLHQPLDGWDL DHGLFTQHIMPD NALDEYFTKPSL 23 Phage display (common panning) 3-4 PMID:19084031 Anti-neuwiedase polyclonal antibodies Zinc metalloproteinase neuwiedase Not determined. Not determined. Ph.D.-12 phage display library (X12) In fact, 80 mimotopes were obtained. However, only 24 mimotopes aligned with the primary structure of neuwiedase were given in the original paper. 572 SKSSITITNKRLTRK 1 Phage display (common panning) 3 PMID:19186111 Anti-SPACc polyclonal antibody IgG Scolex protein antigen from cysticercus cellulosae (SPACc) Not determined. Not determined. G-α phage display library (XXLXXXAX) Four libraries were used in panning against anti-SPACc IgG. Many phage clones were picked and checked. However, only one sequence is given in the original paper. It was showed that SKSSITITNKRLTRK might be devoloped into a promising diagnostics for human neurocysticercosis. 573 SWTWHFPESPPP(9)[+, +, -] SWTFYWPDAQLG(3)[+, +, -] QWQLHWPASKQA(2)[+, +, -] EWTWVFPTTHTS(1)[+, +, -] EWTFQWNSYPAD(1)[+, +, -] EWDFFWPPTQTP(1)[+, +, -] EWQYHWPTLQSR(1)[+, +, -] QWTITYPKPPAL(1)[+, +, -] GWTVFYPDNLRP(1)[+, +, -] QWEWHYMAGYLA(1)[+, +, -] 10 Phage display (common panning) 3 PMID:19465078 Cadherin-1 Cadherin-1 Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The binding of each clone to E-cad/Fc chimeric protein, N-cad/Fc chimeric protein and VE-cad/Fc chimeric protein was confirmed by ELISA, respectively. + denotes phage clone bound to the cadherin ectodomain/Fc chimeric protein and - represents phage clone did not bind to the cadherin ectodomain/Fc chimeric protein. In fact, the target used in the experiment is a chimeric protein composed of the E-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment. The bound phages were eluted through using TBS containing 2 mM EDTA. Total number of clones were 23. All of the phage clones not only bound to the E-cad/Fc chimeric protein, but also to the Ncad/Fc chimeric protein. 574 SWELYYPLRANL(8)[+, +, -][9.4, 0.323] QWEIRYPWPSMG(4)[+, +, -][NT] QWTYYLPLTPRW(2)[+, +, -][NT] EWTYTFPTAHSI(2)[+, +, -][NT] EWFWSWPGYSNT(1)[+, +, -][NT] SWEWYIPYLNRT(1)[+, +, -][NT] AWTWSLPTLPQS(1)[+, +, -][NT] 7 Phage display (common panning) 3 PMID:19465078 Cadherin-1 Cadherin-1 Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA,Surface plasmon resonance (SPR) The binding of each clone to E-cad/Fc chimeric protein, N-cad/Fc chimeric protein and VE-cad/Fc chimeric protein was confirmed by ELISA, respectively. + denotes phage clone bound to the cadherin ectodomain/Fc chimeric protein and - represents phage clone did not bind to the cadherin ectodomain/Fc chimeric protein. Besides, the binding of the linear peptide, H-SWELYYPLRANL-NH2 to E-, N-, P- and OB-cad/Fc chimeric proteins was analyzed by SPR. The linear peptide, H-SWELYYPLRANL-NH2 was found to bind to the E- and N-cad/Fc chimeric proteins with high affinities (Kd, μM) of 9.4 μM and 0.323 μM, respectively. NT denotes not tested. In fact, the target used in the experiment is a chimeric protein composed of the E-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment. The bound phages were eluted through using 0.2M glycine HCl, pH 2.2 followed by neutralization with 1 M Tris-HCl, pH 9.1. Total number of clones were 24. All of the phage clones not only bound to the E-cad/Fc chimeric protein, but also to the Ncad/Fc chimeric protein. Peptide SWELYYPLRANL was found to bind both E- and N-cad/Fc chimeric proteins with affinities (KD) of 9.4 μM and 323 nM, respectively, as judged by surface plasmon resonance spectroscopy. 575 CKRDSTWC(8)[1.8 ± 0.12] CKYLWSKC(4)[1.1 ± 0.08] CKYWWSKC(3)[1.3 ± 0.11] CKYWLSRC(3)[1.05 ± 0.13] CKYAWSRC(1)[0.9 ± 0.05] CKYSMSKC(1)[0.8 ± 0.07] K-[RY]-x-W-S-[KR] 6 Phage display (common panning) 4 PMID:19520204 Anti-rabies virus polyclonal antibody IgG Glycoprotein G Not determined. Not determined. fdMED1-based CX6C M13 phage display library ELISA Absorbance measured at 450nm after substraction of background was shown. The selected mimotopes were able to inhibit the interactions of the human anti-rabies virus IgG antibodies with rabies virus in a dose-dependent manner. Subcutaneous administration of phage bearing CKRDSTWC induced an rabies virus glycoprotein-specific IgG response in BALB/c mice.