<result><BiopanningDataSet><Item><BiopanningDataSetID>1051</BiopanningDataSetID>
<Peptides>NWPRWWEEFVDKHSS(16)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9430247</Reference>
<Target_Name>Anti-gp120 monoclonal antibody b12</Target_Name>
<Template_Name>Surface protein gp120, SU</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f3-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Phages were eluted with recombinant gp120.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1052</BiopanningDataSetID>
<Peptides>HSFGDLSISPNSLTAWPGTLP(3)
FCVRLMCSGLIPFFVLCCFFA(2)
FSRADFFPLSYSLSSVPSTAL(2)
FSFYPPDIVHTTAFSSFVNPVD(1)
SSFFYSALTPSFPSPYSQSSR(1)
RFFAFPMVCASFFLVAIAFFP(1)
PLPPSRFFITVCLTFLFSLSFF(1)
VRPCVASLLLFFCLLFLLLPS(1)
ICFPFNTRYCIFAMMVSSLVF(1)
QQAGSYPGCIDYYYCHASAIG(1)
VRFHLAGWLPAVVSFVIFSDH(1)
DGLRSDGSWLARFVFNGSGFY(1)
FAHEGSASFRLSSKVEDWVSR(1)
RHFVPLYLSVSYDGFSRGASI(1)
PIIHPHPPRIAMRVSISPFP(1)
TPTDSTVRGSSTMDGFLKSVY(1)
TASFWRSVSFPWVLSFLAFSH(1)
GNFTASTASWGDELLALY(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9430247</Reference>
<Target_Name>Anti-gp120 monoclonal antibody b12</Target_Name>
<Template_Name>Surface protein gp120, SU</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X21 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1053</BiopanningDataSetID>
<Peptides>CSEFHFGPHRGVPRGC
CKRIHFGPGRVGGXTC
CVRTHFGPGRVMEVVC
CLMNHLGPGRSARVDC
CRAFHIGPGRGSHRHC
CSAHHVGPGRGRVLWC
CQGIHYGPGRRSQSC
PGMLDGYHYGPGRGS
VAMRGVVHHXPGRYV
KGEREIVXYGPGRVG
CSNFVYGPSRLVQQSC
CIGRLYGPGRVTMSGC
CFKXFLGPGRVAYVDC
CRLVQLGPGRSAAMDC
CRAWWIGPGRSGPEAC
GTVRPAHVFGPGRGL
APVRDRQEFGPGRSR
EEHARIRFFGPGRAG
WFRRYVLMMGPGRWG
CXLIRNGPGRGNTLRC
DAVRAVVRWGPGRAG
CKILRRGPGXISLEHC
AEAPVVVFRGPGRTA
CGVVQRGPGRSVMSDC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>24</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9430247</Reference>
<Target_Name>Anti-gp120 monoclonal antibody 447-52D</Target_Name>
<Template_Name>Surface protein gp120, SU</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX5GPXRX5C bias phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1054</BiopanningDataSetID>
<Peptides>LLREQRYGPGRHNLHPLL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9430247</Reference>
<Target_Name>Anti-gp120 monoclonal antibody 447-52D</Target_Name>
<Template_Name>Surface protein gp120, SU</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>LLX5GPXRX5LL bias phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1055</BiopanningDataSetID>
<Peptides>SGSLVEWGCDHKLMC(1)
GGTAFPQWGCRELWC(1)
EWGCETMRQLCCLPL(2)
DRDYFLGWFTTPSIG(4)
VGHFGDWFKMPPVGS(2)
SWIWGQTFVRAHGRD(1)
QDDWVGWWHFMPAK(2)
DWSWGLHMTRLG(1)
GSGWPWAEA(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9430247</Reference>
<Target_Name>Anti-gp41 monoclonal antibody 50-69</Target_Name>
<Template_Name>Transmembrane protein gp41, TM</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f3-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1056</BiopanningDataSetID>
<Peptides>CNGRCVSGCAGRC(0.26)
CGRECPRLCQSSC(0.15)
CGEACGGQCALPC(0.06)</Peptides>
<Motif>NGR</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:9430587</Reference>
<Target_Name>Mice carrying human MDA-MB-435 breast carcinoma xenografts</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX3CX3CX3C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Endothelial cells in the angiogenic vessels within solid tumors express several proteins that are absent or barely detectable in established blood vessels. CX3CX3CX3C library was screened in mice carrying human MDA-MB-435 breast carcinoma xenografts. Phage displaying CNGRCVSGCAGRC, homed selectively to breast cancer xenografts. This homing can be inhibited by the free CNGRCVSGCAGRC, but not by the CNGRC peptide, even when this peptide was used in amounts 10 times.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1057</BiopanningDataSetID>
<Peptides>CDCRGDCFC(0.80)
CTCVSTLSC(0.05)
CFRDFLATC(0.05)
CSHLTRNRC(0.05)
CDAMLSARC(0.05)</Peptides>
<Motif>RGD</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:9430587</Reference>
<Target_Name>Mice carrying human MDA-MB-435 breast carcinoma xenografts</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Endothelial cells in the angiogenic vessels within solid tumors express several proteins that are absent or barely detectable in established blood vessels, including alphav integrins and receptors for certain angiogenic growth factors. CX7C library was screened in mice carrying human MDA-MB-435 breast carcinoma xenografts. Phage displaying CDCRGDCFC, homed to several tumor types (including carcinoma, sarcoma, and melanoma) in a highly selective manner, and homing is specifically inhibited by the cognate peptide. The embedded motif RGD has been shown to bind selectively to alphav beta3 and alphav beta5 integrins.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1058</BiopanningDataSetID>
<Peptides>CGSLVRC(0.35)
CGLSDSC(0.12)
CYTADPC(0.08)
CDDSWKC(0.08)
CPRGSRC(0.04)</Peptides>
<Motif>GSL</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:9430587</Reference>
<Target_Name>Mice carrying human MDA-MB-435 breast carcinoma xenografts</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX5C phage libray</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Endothelial cells in the angiogenic vessels within solid tumors express several proteins that are absent or barely detectable in established blood vessels. CX5C library was screened in mice carrying human MDA-MB-435 breast carcinoma xenografts. The motif GSL and its permutations were frequently recovered from screenings using breast carcinoma, Kaposi's sarcoma, and malignant melanoma, and homing of the phage was inhibited by the cognate peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1059</BiopanningDataSetID>
<Peptides>WHDWAYW(3)
LPLWAIV(1)
TTWWWQF(1)
SAPWWTF(1)
LPPWAAF(1)
GHTWWTF(1)
KPMWWHF(1)
SWWSFTP(1)
WHSFPPP(1)
WHSFPDS(1)
WHDFPLV(1)
TPTLEAA(1)
SPLNTQR(1)
SPPSAML(1)
QNWWFSF(1)
GWYAFTQ(1)
SWWDFTQ(1)
THLSFLS(1)
YHSFNGT(1)
WHTFDYS(1)</Peptides>
<Motif>W-x(2)-F</Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9525900</Reference>
<Target_Name>Protein Vpr</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Purified and denatured His-tag Vpr produced from baculovirus was used by coating plates as the target protein to screen the binding phage for Vpr interactions.</Brief_Description>
<BiopanningDataSet_Comments>Three rounds of panning were carried out at constant stringency. Peptides specific for the His-tag Vpr binding were selected by eluting with 5 mM reduced glutathione in Tris-buffered saline.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1060</BiopanningDataSetID>
<Peptides>TPWWSFM(2)
SWWSFYP(2)
AWWEFLD(2)
QPWWAFF(1)
SWWSFSM(1)
KWWEFPA(1)
TWWGFPA(1)</Peptides>
<Motif>W-x(2)-F</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9525900</Reference>
<Target_Name>Protein Vpr</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Native GST-Vpr fusion protein was used as a target protein to screen the binding phage for Vpr interactions through binding to beads.</Brief_Description>
<BiopanningDataSet_Comments>Three rounds of panning were carried out at constant stringency. peptides specific for the GST-Vpr binding were selected by eluting with 5 mM reduced glutathione in Tris-buffered saline.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1061</BiopanningDataSetID>
<Peptides>CLLRMSIC(10)
CRLKSRRNC(3)
CLPPPNRRC(2)
CHTLLKSQC(1)
CRRIKPRIC(1)
CTMLNRNMC(1)
CRLIHLMLC(1)
CIRLRXLRC(1)
CPISNRLIC(1)
CPLMRRILC(1)
CRRNRSRKC(1)
CRTRPKRRC(1)
CKPLMSIRC(1)
CRRLRLHRC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11532073</Reference>
<Target_Name>Intercellular adhesion molecule 1, ICAM-1</Target_Name>
<Template_Name>Integrin alpha-L beta-2</Template_Name>
<Structure_of_Target_Template_Complex>1MQ8,3TCX,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Authors used the mAb 84H10 to elute bound phage, because this mAb has previously been shown to bind ICAM-1 and prevent LFA-1 interaction, implying that LFA-1 and 84H10 bind at similar locations on ICAM-1.</Brief_Description>
<BiopanningDataSet_Comments>Fourteen different peptide sequences were identified and analysis of these sequences did not show a consensus sequence. One peptide sequence (*CLLRMRSIC*) was present on 10 of the 26 sequenced phage.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1062</BiopanningDataSetID>
<Peptides>FEGFSFLAFEDFVSSI(2)
RDGWYESVSYWGVIDW(2)
GAEGIEVKYWVDLGWV(1)
FAGAAWHERLGYGHAT(1)
PYRIDAWADVDEMVWM(1)
IFVGAYVVN(1)
FDGFSFLAFEDFVSSI(1)
ILGHTWQALGWLVTGR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:12963036</Reference>
<Target_Name>Intercellular adhesion molecule 1, ICAM-1</Target_Name>
<Template_Name>Integrin alpha-L beta-2</Template_Name>
<Structure_of_Target_Template_Complex>1MQ8,3TCX,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X16 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>To assure a native presentation of the extracellular domains of ICAM-1 we have transfected COS-7 cells with plasmid inserted with cDNA encoding the common form of ICAM-1. The obtained ICAM-1 positive cell subline was used for the screening of the phage library.</Brief_Description>
<BiopanningDataSet_Comments>Several clones contained the X1E/DX3X4SX6X7X8X9X10DX12 motif, where the amino acid distribution at X1 and X12 favored aromatic amino acids, while X3, X4, X6 to X10 seem to be random.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1063</BiopanningDataSetID>
<Peptides>FEGFSFLAFEDFVSSI(10)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:12963036</Reference>
<Target_Name>Intercellular adhesion molecule 1, ICAM-1</Target_Name>
<Template_Name>Integrin alpha-L beta-2</Template_Name>
<Structure_of_Target_Template_Complex>1MQ8,3TCX,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X16 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>To assure a native presentation of the extracellular domains of ICAM-1 we have transfected COS-7 cells with plasmid inserted with cDNA encoding the common form of ICAM-1. The obtained ICAM-1 positive cell subline was used for the screening of the phage library. During which the library was first subtracted on the nontransfected COS-7 cells in each of the four rounds of panning prior to exposing the library to ICAM-1-expressing cells.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1064</BiopanningDataSetID>
<Peptides>CSPQYWTGPAC(12)[1.55 ± 0.51, 0.43 ± 0.11]
CVQFPTSEKMC(1)[1.50, 0.47]
CSDPRKMCIYC(1)[1.86, 0.70]
CIWENAGRMVC(1)[1.95, 0.80]
CHAGTFLQVAC(1)[1.19, 0.29]
CLVAQINLEMC(1)[2.09, 0.88]
CERHTKFPSVC(1)[1.92, 0.70] </Peptides>
<Motif>SPQYWTGPA</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:14728804</Reference>
<Target_Name>CD81 antigen</Target_Name>
<Template_Name>Envelope glycoprotein E2</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>pVIII-9aa.Cys phage display library (CX9C)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage clones binding to MOLT-4 cells were detected by horseradish peroxydase (HRP)-conjugated anti-M13 phage antibody in the absence or presence of anti-hCD81 MAb by ELISA. The absorbance at 450 nm was measured and average values from two independent experiments were determined. The original phage peptide library PVIII9aaCys without selection was used as a negative control and the corresponding A450 values were 0.2 and 0.17. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1065</BiopanningDataSetID>
<Peptides>WTYIPPV[High]
WLYVPPV[ND]
FTYVPHT[ND]
FTYMPPV[High]
FTYMPLP[ND]
FEWVPMI[ND]
FPCFFCY[Very high]
PLPISPR[High]
ATTLLLA[Low]
GSQSHHI[Low]</Peptides>
<Motif>[FYW]-[RNDCEQHKSTY]-[FYW]-[AGILMFPWV]-P</Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:14506253</Reference>
<Target_Name>Chaperone surA</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Contents in the square bracket were based on results of ELISA affinity evaluations. ND represented not determined.</Affinity_Measurement_Description>
<Brief_Description>Mature E. coli SurA protein was expressed as a fusion with a self-cleaving intein.</Brief_Description>
<BiopanningDataSet_Comments>Authors find that both full-length SurA and its core module have similar peptide bind-ing specificities and affinities for peptides with a consensus sequence of the form aromatic-polar-aromatic-nonpolar-proline.
</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1066</BiopanningDataSetID>
<Peptides>WTYIPPV[High]
WEYIPNV[Very high]
WSYIPVV[High]
FNYVPPT[High]
FTYIPNS[High]
FTYIPHT[ND]
FDFNRRI[High]
TAPGVST[Low]</Peptides>
<Motif>[FYW]-[RNDCEQHKSTY]-[FYW]-[AGILMFPWV]-P</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:14506253</Reference>
<Target_Name>SurA (delta-P2)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Contents in the square bracket were based on results of ELISA affinity evaluations. ND represented not determined.</Affinity_Measurement_Description>
<Brief_Description>Mature E. coli SurA protein was expressed as a fusion with a self-cleaving intein.</Brief_Description>
<BiopanningDataSet_Comments>Authors find that both full-length SurA and its core module have similar peptide bind-ing specificities and affinities for peptides with a consensus sequence of the form aromatic-polar-aromatic-nonpolar-proline.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1067</BiopanningDataSetID>
<Peptides>FRDIISGTS(7)
WKDVVSGRH(2)
SIIDGIRAL(1)
ERQVITGRV(1)
GRDIITGRI(1)
ERDIISGIA(1)
IGNIITGTK(1)
TGNVMTGLK(1)
DILDGLK(1)
ERDVVTGRA(1)
RDIITGLLM(1)
DRDIISGRK(1)
FKDITSGTS(1)
NVITGLRHT(1)
TKDIVMGTQ(1)
DRNVITGHS(1)
ERDVVRGTV(1)
NIITGQRQY(1)
YRDVLRGVL(1)
HRDILRGTA(1)
DRNIITGFG(1)
YKDPTRGTD(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>22</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12794137</Reference>
<Target_Name>Anti-b558 monoclonal antibody NL7</Target_Name>
<Template_Name>Cytochrome b-245 heavy chain</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>J404 phage display library (X9)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Epitope mapping by phage display analysis indicated that NL7 binds the 498 EKDVITGLK 506 region of gp91phox. Each selected peptide shown contains from four to eight residues similar to those of the identified epitope.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1068</BiopanningDataSetID>
<Peptides>FHFNPYTGHPLT(2)[1.09 ± 0.07]
KVVPPWHSVLPG(1)[0.05]
SPKLLTNWHLLI(1)[0.06]
HNWGGSDFWSFG(1)[0.08]
FDPNNYWTPMGR(1)[0.08]
TDMQFPGFHAAL(1)[0.10]
EYPDPPAWHLWF(1)[0.10]
WSATWTLSDTWK(1)[0.10]
YTTPPFHTGWIW(1)[0.10]
YHAGRVNTMSWL(1)[0.10]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:12199523</Reference>
<Target_Name>Monoclonal antibody 5E8</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Optical densities at 415 nm were measured with an automated ELISA plate reader. The value of the peptide FHFNPYTGHPLT was expressed as mean ± SD. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These 11 clones were subjected to analysis by phage ELISA. Only FHFNPYTGHPLT clones were found to be reactive to MoAb 5E8 but not to control anti-FLAG M2 MoAb in the ELISA assay. We compared this peptide sequence with those of dipeptidyl peptidaseIV (DPPIV,E.C.3.4.14.5) and Cell-CAM105, which proteins were located by a database search based on the information of tissue localization and approximate molecular weight of the MoAb 5E8 antigen, and sequence similarity with a region in DPPIV (aminoacids225-233) but not with Cell-CAM105 was found.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1069</BiopanningDataSetID>
<Peptides>MHNHHNHPRPSS[0.56 ± 0.05]
MHSDMHAPVSDI[0.91 ± 0.10]
HTKPHAWHLMSH[0.25 ± 0.03]
HTMYYHHYQHHL[0.99 ± 0.06]
LPNPISPRWWVG[0.35 ± 0.02]
CDPLLKHHTHPK[0.33 ± 0.11]
NHPAVVEPAPSL[0.50 ± 0.03]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:12183450</Reference>
<Target_Name>Kinase domain of VEGFR2</Target_Name>
<Template_Name>Vascular endothelial growth factor A, VEGF-A</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 492 nm was measured. Data shown are the mean ± S.D. of three independent experiments and reproduced from the graph. </Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>A novel peptide designated K237-(HTMYYHHYQHHL), which was isolated from a phage-displayed peptide library, binded to KDR with high affinity and specificity. By interfering with the VEGF-KDR interaction, the peptide K237 inhibited proliferation of cultured primary human umbilical vein endothelial cells induced by recombinant human VEGF165 in a dose-dependent and cell type-specific manner.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1070</BiopanningDataSetID>
<Peptides>FGGETFTPDWMMEVAIDNE(3)
ASSEEETPAWMMEGVFEAW(3)
KMGEEFTPDWMMESDFQGW(1)
EKQDWYTPEWMMEEGWTVW(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:12471134</Reference>
<Target_Name>Anti-GXM monoclonal antibody 2H1</Target_Name>
<Template_Name>Glucuronoxylomannan, GXM</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>L200 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1071</BiopanningDataSetID>
<Peptides>KMGGTNHPE(2)
KSAVTNHGI(2)
HLNHPMSIM(1)
KYKFEEVWR(4)
KMAFQDVWM(2)
KSGFNEVWP(1)</Peptides>
<Motif>K-x(3)-T-N-H-P, K-x(2)-F-x-[ED]-V-W</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11786117</Reference>
<Target_Name>Proximal convoluted tubules, PCT</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>LL9 phage display library (X9)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1072</BiopanningDataSetID>
<Peptides>CKDTSWLGEWLC(4)
CEKSSWLAEWLC(2)
CLLTSFLGEVYC(1)
CLISQRHVASSC(1)</Peptides>
<Motif>C-[TS]-S-W-L-[AG]-E-W-L-C</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11786117</Reference>
<Target_Name>Proximal convoluted tubules, PCT</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CL10 phage display library (CX10C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1073</BiopanningDataSetID>
<Peptides>MGSHIEPGG(4)
TGSFGVAGG(2)
GGMVSQGSK(1)
GGMGEHGSS(1)</Peptides>
<Motif>G-[GS]-x(4)-G-[GS]</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:11786117</Reference>
<Target_Name>Proximal convoluted tubules, PCT</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>LL9 phage display library (X9)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In an attempt to deplete the linear nonapeptide library LL9 of ligands binding unspecifically to different neph-ron segments, we incubated a library aliquot with isolated CCD prior to panning unbound phage on microdissected PCT.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1074</BiopanningDataSetID>
<Peptides>GVKGVQGTL(3)
HGVRGNLIS(2)
GVRGQLATP(1)
GMRDHRMTI(4)
ETMQRDVRA(2)
RDFRDIWA(1)
SLRDRGFT(1)
HLNMWRDGG(1)
GGAIKDTQN(1)</Peptides>
<Motif>G-V-[KR]-G-x(3)-[TS], R-D-x-R</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:11786117</Reference>
<Target_Name>Proximal convoluted tubules, PCT</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>LL9 phage display library (X9)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In an attempt to deplete the linear nonapeptide library LL9 of ligands binding unspecifically to different neph-ron segments, we incubated a library aliquot with isolated HEK-293 cells prior to panning unbound phage on microdissected PCT.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1075</BiopanningDataSetID>
<Peptides>CAPGPSKSC(4)[NT]
CPHPGTRHC(3)[NT]
CSQYPSRSC(2)[NT]
CEHFFSRSC(2)[NT]
CLNNSQAHC(2)[NT]
CNQRHQMSC(1)[0.301, 0.172]
CNHRYMQMC(1)[0.351, 0.182]
CTPYPSKSC(1)[NT]
CLMTPSKRC(1)[NT]
CQEPTRLKC(1)[NT]
CKEPTRAHC(1)[NT]
CTNTGHRHC(1)[NT]
CPGKISRSC(1)[NT]
CPNNKSASC(1)[NT]
CMNQRVQNC(1)[NT]
CMNQTPDLC(1)[NT]
CTNQFLQQC(1)[NT]
CTKMRLEC(1)[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:14578186</Reference>
<Target_Name>Atherosclerotic lesion surfaces</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The synthetic peptides with homology to TIMP-2 bind to endothelial cells in a dose-dependent manner. Binding of peptides (0.5 μmol/L) was inhibited by purified TIMP-2 protein (0.05 μmol/L), indicating that the peptides mimicking TIMP-2 binding are consistent with a novel binding site for TIMP-2 protein on the surface of these cells. The scrambled control peptide did not bind. The absorbance at 405 nm in the absence or presence of TIMP-2 protein was reproduced from the graph and shown. NT represents no tested.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Through repeated biopanning, 103 peptidyl sequences were identified, many are homologous to known proteins.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>