<result><BiopanningDataSet><Item><BiopanningDataSetID>451</BiopanningDataSetID>
<Peptides>CAPRIGLSC(1)
CLGRPSTVC(1)
CQKSPTNIC(1)
CTKPIPHSC(1)
CTSSAHRYC(1)
CPSRSASHC(1)
CLKSNLARC(1)
CHETRSTIC(1)
CEPTLYSMC(1)
CPTKSHGTC(1)
CKPSPTHGC(1)
CDSRWQTLC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18654983</Reference>
<Target_Name>Chymotrypsinogen A</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Heptamer sequences isolated from biopanning in buffer.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>452</BiopanningDataSetID>
<Peptides>CPGSQRALC(2)
CTDPAKKQC(1)
CLTSGMTQC(1)
CMTKLQKSC(1)
CNSSHAKLC(1)
CQQNNHRHC(1)
CYSHGPQKC(1)
CTTSLHPNC(1)
CEHSTGRYC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18654983</Reference>
<Target_Name>Chymotrypsinogen A</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Heptamer sequences isolated from biopanning in 50% acetonitrile (ACN).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>453</BiopanningDataSetID>
<Peptides>CPWRAPGLC(1)
CFPHETYQC(1)
CHPFHPYVC(1)
CNPHHLHSC(1)
CTTVSHSTC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18680214</Reference>
<Target_Name>Chitinase A</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>CPWRAPGLC was proved to be an inhibitor of chitinase A.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>454</BiopanningDataSetID>
<Peptides>CRGLSHACG(3)
CRHCDSPHG(2)
CMRGIWTLC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18680214</Reference>
<Target_Name>Chitinase B</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>CRHCDSPHG and CRGLSHACG were proved to be inhibitors of chitinase B.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>455</BiopanningDataSetID>
<Peptides>CHETTLRRC(2)
CELPALRLC(1)
CLQDHSPFC(1)
CDLYDSLSC(1)
CMKSHRDKC(1)
CAPFAHATC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 2,(5μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 3,(5μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG].</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>456</BiopanningDataSetID>
<Peptides>CWPGWDLNC(7)
CSLKASFNC(1)
CSWWTLSSC(1)
CGTRPAPFC(1)</Peptides>
<Motif>C-W-P-G-W-x(2)-C</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG]; round 2,(5μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG]; round 3,(5μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG].</Brief_Description>
<BiopanningDataSet_Comments>The strongest binding clone CWPGWDLNC competed with IgG for binding to FcγRIIa and was inhibited from binding to FcγRIIa by the FcγRIIa-blocking antibody, suggesting that CWPGWDLNC and IgG share related binding sites on FcγRIIa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>457</BiopanningDataSetID>
<Peptides>CWPGWDLLC(6)
CWPGWDLNC(1)
CWPGWDEMC(1)
CWPGWDMAC(1)
CSERPSQQC(1)</Peptides>
<Motif>C-W-P-G-W-x(2)-C</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 2,(5μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[1mM DTT]; round 3,(5μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[1mM DTT].</Brief_Description>
<BiopanningDataSet_Comments>The strongest binding clone CWPGWDLNC competed with IgG for binding to FcγRIIa and was inhibited from binding to FcγRIIa by the FcγRIIa-blocking antibody, suggesting that CWPGWDLNC and IgG share related binding sites on FcγRIIa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>458</BiopanningDataSetID>
<Peptides>CTGQRTLYC(3)
CWPGWDLNC(2)
CPTALRIQC(2)
CMPTTLGTC(1)</Peptides>
<Motif>C-W-P-G-W-x(2)-C</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 2,(100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 3,(100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG].</Brief_Description>
<BiopanningDataSet_Comments>The strongest binding clone CWPGWDLNC competed with IgG for binding to FcγRIIa and was inhibited from binding to FcγRIIa by the FcγRIIa-blocking antibody, suggesting that CWPGWDLNC and IgG share related binding sites on FcγRIIa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>459</BiopanningDataSetID>
<Peptides>CHIFQPLHC(1)
CYDKQHSTC(1)
CKLHLSKSC(1)
CLPHSPRSC(1)
CTSQKHLSC(1)
CDLWFHPNC(1)
CFTGYPPNC(1)
CSQSQQPPC(1)
CNALGMPIC(1)
CNGPLFNIC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){nil}[0.1 mg/ml IgG]; round 2,(100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[1mM DTT]; round 3,(100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[1mM DTT].</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>460</BiopanningDataSetID>
<Peptides>CWPGWDLNC(4)
CWPGWDLLC(1)
CTGQRTLYC(1)
CPTALRIQC(1)
CQNSARQQC(1)
CHAIWRSIC(1)</Peptides>
<Motif>C-W-P-G-W-x(2)-C</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17673295</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</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>In fact, the recombinant fusion protein HSA-FcγRIIa was used as the target. However, HSA-binding phages were removed using human serum albumin. For each round, panning parameters were wrote as (target) {wash} [elution]. Round 1, (100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG]; round 2,(100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG]; round 3,(100μg/ml HSA–FcγRIIa){0.1 mg/ml IgG}[10 mg/ml IgG].</Brief_Description>
<BiopanningDataSet_Comments>The strongest binding clone CWPGWDLNC competed with IgG for binding to FcγRIIa and was inhibited from binding to FcγRIIa by the FcγRIIa-blocking antibody, suggesting that CWPGWDLNC and IgG share related binding sites on FcγRIIa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>461</BiopanningDataSetID>
<Peptides>CTLPHLKMC(10)
CLYGNSDKC(3)
CQHNHSKQC(3)
CTKQHTSQC(3)
CNPSLALHC(3)
CSTGAHTQC(3)
CDWTKPQSC(2)
CTVKNGTLC(1)
CQEGKMRLC(1)
CSEHKTPMC(1)
CQKQGHPSC(1)
CTSTPFRIC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18442789</Reference>
<Target_Name>Human B cell Burkitt lymphoma cell line Raji</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>MALDI-TOF mass spectrometry following immunoprecipitation assay showed that a potential template for the peptide CTLPHLKMC is a variable region of human immunoglobulin heavy chain which would be a specific phenotypic marker of Raji.</Brief_Description>
<BiopanningDataSet_Comments>The phage clone encoding CTLPHLKMC peptide sequence avidly bound to Raji cells compared with control phage clones. Furthermore, flow-cytometric analysis on the biotinylated synthetic CTLPHLKMC peptide demonstrated the high binding affinity to Raji cells in a dose-dependent manner whereas it has binding activity to neither human peripheral bloodmononuclear cells including normal B cell derived from healthy donors nor other leukemia cells including THP-1, HL-60, Jurkat and IM-9.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>462</BiopanningDataSetID>
<Peptides>SWTLYTPSGQSK(4)
HWYITTGPVREK(3)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18655820</Reference>
<Target_Name>Cadherin-2</Target_Name>
<Template_Name>Cadherin-2</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In fact, the target used in the experiment is a chimeric protein composed of the N-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment. The bound phages were eluted through adding 100 ml TBS containing 2 mM EDTA to each well and incubating for 10 min at room temperature with constant agitation.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>463</BiopanningDataSetID>
<Peptides>NWFIDFPVYPPL(7)
SWTLYTPSGQSK(6)
AWQVHYSYVASS(2)
KWELTYFANSFP(1)
EWMIHYDSALTS(1)
SWLAVWPATGAS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18655820</Reference>
<Target_Name>Cadherin-2</Target_Name>
<Template_Name>Cadherin-2</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In fact, the target used in the experiment is a chimeric protein composed of the N-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment. The bound phages were eluted through adding 100 ml 0.2M glycine HCl to each well and incubating for 10 min at room temperature with constant agitation followed by neutralization with 1 M Tris-HCl, pH9.1 (20 ml/well).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>464</BiopanningDataSetID>
<Peptides>CSERQALHGWC
CDEKRALHNLC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18363340</Reference>
<Target_Name>Platelet glycoprotein Ib alpha chain</Target_Name>
<Template_Name>von Willebrand factor (vWF)</Template_Name>
<Structure_of_Target_Template_Complex>1M10,1SQ0,1U0N,4C2A,4C2B,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX9C M13 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>465</BiopanningDataSetID>
<Peptides>CNERAALWNLC
CTERWALHNLC
CESRWWLRNAC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18363340</Reference>
<Target_Name>Platelet glycoprotein Ib alpha chain</Target_Name>
<Template_Name>von Willebrand factor (vWF)</Template_Name>
<Structure_of_Target_Template_Complex>1M10,1SQ0,1U0N,4C2A,4C2B,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX9W1-9C M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>CTERWALHNLC inhibited GPIbA-vWF-mediated platelet aggregation induced under high shear conditions.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>466</BiopanningDataSetID>
<Peptides>HQPANDPSWYTG
NTISGLRYAPHM</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18067293</Reference>
<Target_Name>Tetragonal BaTiO3</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Tetragonal BaTiO3 powder (99.9% purity) was used as the target.</Brief_Description>
<BiopanningDataSet_Comments>These peptides can induce the room-temperature formation of ferroelectric (tetragonal) BaTiO3 within 2 h from an aqueous precursor solution at near neutral pH.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>467</BiopanningDataSetID>
<Peptides>CSKSSDYQC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18440083</Reference>
<Target_Name>Rat small intestinal mucosal tissue</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The Ph.D.-C7C library was orally administered into overnight-starved, 12-week-old male Sprague-Dawley (SD) rats. After 1h retention, rats were sacrificed and phages from four representative organs (liver, lung, spleen, and kidney) were eluted and amplified for next round of panning. After the third round of biopanning, total 850 peptide sequences were determined from randomly selected individual phage recombinants from four representative organs, liver (from which 220 peptide sequences were identified), lung (218), spleen (204), and kidney (208).</Brief_Description>
<BiopanningDataSet_Comments>CSKSSDYQC was the peptide ligand which appeared 9 times (thrice in liver; twice in lung, spleen, and kidney) out of total 850 sequences selected by in vivo phage display. Phages displaying CSKSSDYQC showed a significantly higher affinity to small intestinal mucosal tissue compared with the native M13 phage.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>468</BiopanningDataSetID>
<Peptides>VPGQKQHYVQPTAAN(23)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18462752</Reference>
<Target_Name>Secretion chaperone</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>f88-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>CsaA from Agrobacterium tumefaciens (AtCsaA) was biotinylated and used as the target. The initial library was incubated overnight with the streptavidin magnetic beads to remove streptavidin binding phage.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-three clones were sequenced after the third round of selection. All clones had the same sequence VPGQKQHYVQPTAAN. The atomic coordinates of the AtCsaA structure with the bound peptide has been deposited in the PDB with the ID 2Q2H; the PDB ID for the AtCsaA structure without the peptide is 2Q2I.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>469</BiopanningDataSetID>
<Peptides>CGIKVATQTQRC
CRRKPEPLLPNC
CPPVDRRHVAAC
CMKRSPNEPHHC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18462752</Reference>
<Target_Name>Secretion chaperone</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>LX10 phage display library (CX10C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>CsaA from Agrobacterium tumefaciens (AtCsaA) was biotinylated and used as the target. The initial library was incubated overnight with the streptavidin magnetic beads to remove streptavidin binding phage.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>470</BiopanningDataSetID>
<Peptides>AHVELMM(1)
LTLAGAS(1)
NVDGAVS(1)
IAPTNGP(1)
AENITTK(1)
QQYDPMH(1)
ALNMAPH(1)
NTSPVPK(1)
SFQLFHG(1)
TWPYYPN(1)
SAFDNPY(1)
TRLNIPP(1)
HSPPAMR(1)
FNTLNSI(1)
QLDTRLL(1)
LPLNPLL(1)
MLPHPTP(1)
AETVKVV(1)
STPRNSS(1)
SPQQASA(1)
VLTTRLA(1)
WSPLHNT(1)
ALLDPTV(1)
YPGYFTK(1)
YSKPSQM(1)
YHYKTTS(1)
HNFNVPF(1)
SDNVKWN(1)
AATPSEG(1)
FTSSPSP(1)
TSTVTHV(1)
AADNTSG(1)
ASSLRSV(1)
SFKPAMH(1)
NDPWQFH(1)
TATDLSP(1)
MYTSPLS(1)
NMSGPLP(1)
ADAITIG(1)
HAYATFQ(1)
QSPAAQP(1)
KLPPSFP(1)
MTSHTSG(1)
LPKPWLN(1)
GEVRTHA(1)
GQFKLTK(1)
AETVESC(1)
STAGPVG(1)
NAEGVRL(1)
SIRLPSP(1)
NNSMPGP(1)
NTRLPVI(1)
SKTDIPN(1)
KSPPLMQ(1)
AQVDVTV(1)
HPSSYWT(1)
FKMPLIS(1)
LQTNWYS(1)
RAPTPPF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>59</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:18602466</Reference>
<Target_Name>Mouse digestive tract</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>The Ph.D.-7 library was orally administered into 2 Swiss albino male mice weighing 25g. One hour later, phages passed through the intestinal barrier was evaluated by investigating its presence in the samples prepared from spleen. Statistical treatment of the obtained sequences did not support the notion that the GI translocation depends on the presence of any particular peptide sequence fused on the pIII coat proteins of the M13 phages.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>471</BiopanningDataSetID>
<Peptides>APLLSSK(1)
WHLPRPI(1)
DVPAPKP(1)
IRSPASY(1)
DNRHSTP(1)
SNYAVLL(1)
HQNHNLS(1)
AVYSPSR(1)
TLPTIFH(1)
AAGNRLP(1)
SYTPYQP(1)
NPPHLAS(1)
FTSQAPT(1)
DSLTARL(1)
LPLHPVH(1)
THLMSPI(1)
STVSSMR(1)
DHLVTAP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:18602466</Reference>
<Target_Name>Mouse digestive tract</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>The Ph.D.-7 library was orally administered into 2 Swiss albino male mice weighing 25g. One hour later, phages passed through the intestinal barrier was evaluated by investigating its presence in the samples prepared from blood. Statistical treatment of the obtained sequences did not support the notion that the GI translocation depends on the presence of any particular peptide sequence fused on the pIII coat proteins of the M13 phages. </Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>472</BiopanningDataSetID>
<Peptides>CLEVSRKNC(9)
CKRGGATAC(7)
CRSAVAKNC(5)
CTKRNAPDC(3)</Peptides>
<Motif></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:18692101</Reference>
<Target_Name>Ischemic stroke tissue from transient middle cerebral artery occlusion model</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 T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Phage library displaying CX7C random peptides on the viral surface was injected into the tail veins of Adult male Sprague-Dawley rats at 4h following ischemic injury and allowed to circulate for 2h. The ipsilateral (ischemic) hemisphere of each brain was removed and the tissue-bound phages were recovered and amplified for the next round of screening. After three rounds of screening, the titers of recovered phages were enriched by approximately 60-fold. Thirty phage clones from the second and third round were randomly picked and sequenced.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>473</BiopanningDataSetID>
<Peptides>NPVENMMDRDSQ(32)
NPVEWFMSTVNT(16)
NPVESWLTHTRI(10)
NPVEHAVNALRP(2)
NPVETYTGLYHV(2)
NPVEGMLTVLAR(1)
NPVEIALTVPTR(1)
NPVEHFLSAKLW(1)
NELVIPNITPAR(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples before rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by pH-shift using glycine-HCl, pH 2.2. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>474</BiopanningDataSetID>
<Peptides>NPIEALM(1)
NPVETQV(1)
NPVEMLL(1)
NPVEHMM(1)
NPVESLL(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples before rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</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>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by pH-shift using glycine-HCl, pH 2.2. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>475</BiopanningDataSetID>
<Peptides>CPEVDRATC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples before rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by pH-shift using glycine-HCl, pH 2.2. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>