<result><BiopanningDataSet><Item><BiopanningDataSetID>401</BiopanningDataSetID>
<Peptides>GQPTPRNAGLPL(3)
SRLNVEPLTTYS(2)
TTLHWASLTTGR(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17136792</Reference>
<Target_Name>Gonadotropin-releasing hormone promoter (GP) </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>GP (from -813 to -1081) was immobilized on the surface of Streptavidin MagneSphere Paramagnetic Particles. The beads-DNA complex were then incubated with the library.</Brief_Description>
<BiopanningDataSet_Comments>Twenty clones were sequenced and 16 unique sequences were got. However, sequences appeared only once were not given in the original paper.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>402</BiopanningDataSetID>
<Peptides>QSNPIHIITNTRNHP(3)
KSNPIHIIQNRRNIP(2)
KSNPIHIIKNRRNIP(2)
SPKTTQPPNHIHSIP(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17577983</Reference>
<Target_Name>Human rotavirus</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>f3-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Human rotavirus was cultured in MA104 cells. The purified rotavirus particles immobilized on solid phase were used for panning.</Brief_Description>
<BiopanningDataSet_Comments>These 4 peptides could specifically bind with rotavirus particles. The first 3 peptides can inhibit rotavirus infecting in vitro. QSNPIHIITNTRNHP showed the best efficiency-93% neutralization infectivity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>403</BiopanningDataSetID>
<Peptides>FQHPSFI(14)
PLPTLPL(13)
LPPQSFH(8)
ATYQHAT(3)
WAESKTF(2)
HSALPKW(2)
VSFPFGF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17622312</Reference>
<Target_Name>Hepatocellular carcinoma cell line HepG2</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 normal liver cell line (L-02) was used firstly to carry out subtractive screening.</Brief_Description>
<BiopanningDataSet_Comments>FQHPSFI was shown to bind to the hepatocellular carcinoma cell lines (HepG2 and BEL-7402) and biopsy specimens, but not to normal hepatocytes, other different cancer cells, or nontumor liver tissues.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>404</BiopanningDataSetID>
<Peptides>KTYQGPL(3)
FSPEIRN(3)
VHLGYAT(1)
PHLNYSR(1)
ANHTSPV(1)
PHPLYQS(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:17332091</Reference>
<Target_Name>Colon cancer cell line SW480</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 phages bound to SW480 were treated with normal human intestinal epithelial cells for 2 rounds to eliminate the nonspecific phages.
</Brief_Description>
<BiopanningDataSet_Comments>About 50 clone were sequenced. Only these sequences were given in the original paper. VHLGYAT was shown to be the most effective peptide in targeting SW480, HT29 cells and tumor tissues but not the normal human intestinal epithelial cells and control colon tissue. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>405</BiopanningDataSetID>
<Peptides>QHKTSITGHHLEP
TLPSPLALLTVH
YLFSVHWPPLKA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17947467</Reference>
<Target_Name>Hepatocyte growth factor receptor</Target_Name>
<Template_Name>Hepatocyte growth factor</Template_Name>
<Structure_of_Target_Template_Complex>1SHY, 4K3J,4O3T,4O3U,</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>S114 (NIH 3T3, transfected with the human genes for HGF/SF and Met) and SK-LMS-1/HGF (human leiomyosarcoma cell line autocrine for human Met and human HGF/SF) cells were used alternately to screen the library. NIH 3T3 cells were used for negative selection to remove nonspecific binders. Thus, the target molecule was thought to be Met. Since the three sequenced clones were able to compete with HGF in a dose-dependent manner, their template should be HGF.</Brief_Description>
<BiopanningDataSet_Comments>Thirty phage clones were picked randomly, all of which were found reactive against Met recombinant protein. They were then tested by competitive ELISA with or without HGF for Met binding. Three clones with the ability to compete with HGF in a dose-dependent manner for Met binding were sequenced. YLFSVHWPPLKA displayed the highest competitive ability (59.3% inhibition).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>406</BiopanningDataSetID>
<Peptides>EDYELMDLLAYL(0.95)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:17504878</Reference>
<Target_Name>Thyroid follicular carcinoma cell line FRO82-2</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>The human embryonic kidney cell line 293 cells were used for a negative selection.</Brief_Description>
<BiopanningDataSet_Comments>Among 20 clones sequenced, 95% of all peptides showed the same sequence: EDYELMDLLAYL.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>407</BiopanningDataSetID>
<Peptides>WRQTRKD(18)
WHWRLPS(7)
HAIYPRH(6)
LRQTRKD(4)
LPWHKHR(4)
FHRHHNH(4)
HFFHRHT(3)
HWRHNHS(3)
WPFHHHR(3)
WHHKHRS(3)
WPWHKHS(2)
HKRPRNN(2)
HFTTRQR(2)
MPHIHRH(2)
PRRESRF(2)
KPAPRVH(2)
KHTVTRR(2)
HKTEHPA(1)
HRSPHTP(1)
SWRHHHH(1)
SYSNWTP(1)
QPPIYSA(1)
QPPNYNA(1)
KPRAGSF(1)
KGPHTQV(1)
IASGNSL(1)
IPTLPSS(1)
PTHRHRT(1)
TAPGVST(1)
LGPHTQV(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>30</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18221017</Reference>
<Target_Name>Arabidopsis Fip1 ortholog encoded by At5g58040 (AtFip1[V])</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>Selection were carried out using the N-terminal 137 amino acids of AtFip1[V] as a target. A search of the Arabidopsis proteome using these Fip1-binding peptides as queries resulted in the identification of a number of putative Fip1-interacting proteins. One of these was the polyadenylation factor subunit, CstF77. This purported interaction was confirmed by yeast two-hybrid and in vitro assays. Mutation of the motif identified in the phage display screen eliminated the interaction, corroborating the results of the phage display screen.</Brief_Description>
<BiopanningDataSet_Comments>Eighty-two clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>408</BiopanningDataSetID>
<Peptides>WTITKHP(8)
WRQTRKD(5)
HAHTIST(5)
KPVQLDH(3)
HKRPRNN(2)
ERYMGLP(2)
IQLHPQH(1)
SLDALLS(1)
HAIYPRH(1)
LVGNYTP(1)
SILPYPY(1)
TAPHPVL(1)
HWRHNHS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18221017</Reference>
<Target_Name>Arabidopsis Fip1 ortholog encoded by At5g58040 (AtFip1[V])</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>Selection were carried out using the N-terminal 137 amino acids of AtFip1[V] as a target. A search of the Arabidopsis proteome using these Fip1-binding peptides as queries resulted in the identification of a number of putative Fip1-interacting proteins. One of these was the polyadenylation factor subunit, CstF77. This purported interaction was confirmed by yeast two-hybrid and in vitro assays. Mutation of the motif identified in the phage display screen eliminated the interaction, corroborating the results of the phage display screen.</Brief_Description>
<BiopanningDataSet_Comments>Thirty-two clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>409</BiopanningDataSetID>
<Peptides>WSYSWDGFW(6)
SHLTWDGTW(6)
YTVAWDGTW(3)
LTTEWSGTW(2)
GRLQWDGAW(2)
KSYEWPGTW(2)
MRTEWTGVW(2)
RSIEWSGLW(1)
KSASWDGLW(1)
VVIQWDGAW(1)
RTVEWSGNW(1)
AKTVWDGRW(1)
KSLLTTMAS(1)
GWGMEALGA(1)
RSPN(1)</Peptides>
<Motif>W-x-G-x-W</Motif>
<Unique_Sequence_Number>15</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18200546</Reference>
<Target_Name>Glioma cell line 9L</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>Rat plasma was used as adsorbent before the first round. Before the the second and each subsequent round of panning, phages were preadsorbed on rat blood cells.</Brief_Description>
<BiopanningDataSet_Comments>After the fourth and fifth panning rounds, 15 randomly selected phage clones were propagated and sequenced. RSIEWSGLW-coupled liposomal nanocarriers enhanced drug uptake by 9L cells by 500% compared with conventional liposomal nanocarriers, and significantly increased cytotoxicity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>410</BiopanningDataSetID>
<Peptides>CRGDNFQC(9)
CDVFTYWMRRDC(9)
CDVFEVWMGRVC(4)
CRGTQNTMRARC(1)</Peptides>
<Motif>D-V-F-x(2)-W-M-x-R-x</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18200546</Reference>
<Target_Name>Glioma cell line 9L</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>CL6 phage display library (CX6C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Rat plasma was used as adsorbent before the first round. Before the the second and each subsequent round of panning, phages were preadsorbed on rat blood cells.</Brief_Description>
<BiopanningDataSet_Comments>After the fourth and fifth panning rounds, 15 randomly selected phage clones were propagated and sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>411</BiopanningDataSetID>
<Peptides>QMAFYSHHRSSP
VPQGSFYSSWYT
QSLPQMRFYDS</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:18700874</Reference>
<Target_Name>Anti-ACE monoclonal antibody CG1</Target_Name>
<Template_Name>Angiotensin-converting enzyme, ACE</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>CG1 was selected from hybridomas, which were developed from mice immunized with soluble recombinant human tACE purified from culture medium of CHO cells. Its isotype: IgG1,</Brief_Description>
<BiopanningDataSet_Comments>Seven phage clones were isolated and sequenced. However, only the above three squences were given. Their occurrences were not clear.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>412</BiopanningDataSetID>
<Peptides>LPQQLGKLLACC
WCCAGKHTVTHS
FGCLGKLVCDPPY
MCQGKNICTTIQ
LPCHSKYPCIAS
IGMCKMKAPCAT
YQCERKAPCSTY
LLACTMKLPCSV
ALQCQYKVPCLV
HLSICDSKLICH
ISMCKEKEVCQT
STCSAKGMCTTW
TPCTYKMTCTTK</Peptides>
<Motif>C-x(2)-K-x(2)-C</Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17046088</Reference>
<Target_Name>Anti-B-subtype HIV-1 polyclonal antibody pre-HAART IgG from Patient 1</Target_Name>
<Template_Name>Envelope glycoprotein gp160</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 template should be gp41 since the mimotopes are similar to CSGKLIC of gp41.</Brief_Description>
<BiopanningDataSet_Comments>Among 33 sequenced clones, 26 clones have CXXKXXC motif with 13 unique sequences. Seven sequences without CXXKXXC motif were not shown in the original articles.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>413</BiopanningDataSetID>
<Peptides>HACTGKLRCTTT
THQCLGKLQCGV
LPQQLGKLLACC
WCCAGKHTVTHS
HLSICDSKLICH
ACCTFKNVTTKP
SMCSLKTACTTA</Peptides>
<Motif>C-x(2)-K-x(2)-C</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:17046088</Reference>
<Target_Name>Anti-B-subtype HIV-1 polyclonal antibody  post-HAART IgG from Patient 1</Target_Name>
<Template_Name>Envelope glycoprotein gp160</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 template should be gp41 since the mimotopes are similar to CSGKLIC of gp41.</Brief_Description>
<BiopanningDataSet_Comments>Among 30 sequenced clones, 13 clones have CXXKXXC motif with 7 unique sequences. Seventeen sequences without CXXKXXC motif were not shown in the original articles.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>414</BiopanningDataSetID>
<Peptides>HACTGKLRCTTT
LPQQLGKLLACC
DVCMGKLVCTML
LLACTMKLPCSV
HLSICDSKLICH
YGCHSKITCTTF
TICSMKSACTTW
SPNCEGKIICGS</Peptides>
<Motif>C-x(2)-K-x(2)-C</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:17046088</Reference>
<Target_Name>Anti-B-subtype HIV-1 polyclonal antibody pre-HAART IgG from Patient 3</Target_Name>
<Template_Name>Envelope glycoprotein gp160</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 template should be gp41 since the mimotopes are similar to CSGKLIC of gp41.</Brief_Description>
<BiopanningDataSet_Comments>Among 61 sequenced clones, 16 clones have CXXKXXC motif with 8 unique sequences. Forty-five sequences without CXXKXXC motif were not shown in the original articles.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>415</BiopanningDataSetID>
<Peptides>CSDSWHYWC(10)
CSDWQHPWC(8)
CSDYNHHWC(4)
CSDGQHYWC(2)
CYDSWHYWC(1)
CFDGNHIWC(1)
CTDFPRSFC(1)
CTQDRQHPC(1)
CLSRYLDQC(1)</Peptides>
<Motif>C-S-D-x(2)-H-x-W-C</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:17517791</Reference>
<Target_Name>Vascular endothelial growth factor receptor 3, VEGFR-3</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>Human IgG1 Fc was used firstly to remove Fc-binding phages.</Brief_Description>
<BiopanningDataSet_Comments>The phage displaying peptide CSDSWHYWC exhibited the highest affinity to VEGFR-3 in phage ELISA and the chemically synthesized CSDSWHYWC could bind to VEGFR-3 specifically in a dose-dependent manner. In addition, the flow cytometry assay and immunoflourescence showed that the FITC labelled CSDSWHYWC could bind to VEGFR-3 positive carcinoma cells with specificity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>416</BiopanningDataSetID>
<Peptides>CIGSPSTNC(14)
CSFHYQNRC(3)
CRQSRKRPC(1)
CSRTSSRTC(1)
CELSPSSRC(1)
CTRWAGRPC(1)
CLKRSKLRC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:17097662</Reference>
<Target_Name>Anti-mycobacterial HSP60 polyclonal antibody</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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>417</BiopanningDataSetID>
<Peptides>CNPNNLSHC(1)
CKNFTHTDC(1)
CTTASGARC(1)
CTDLLPRHC(1)
CPTAPLHMC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17482566</Reference>
<Target_Name>Paracetamol(4-acetamidophenol, 4AAP)</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>The identified NPNNLSH-phage clone displayed functional binding properties against paracetamol in solution, able in a peptide sequence-dependant manner to prevent the in vitro hepatotoxicity of paracetamol and reduce (~20%) the permeability of paracetamol across a semi-permeable membrane.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>418</BiopanningDataSetID>
<Peptides>CNPNNLSHC(1)
CRAPSQTVC(1)
CDGNSRTQC(1)
CTTLTKTFC(1)
CTLRSATAC(1)
CSHLHSPLC(1)
CENTQKNSC(1)
CSQGRLGQC(1)
CDRNGSNAC(1)
CSQHSSRSC(1)
CLNSHLQTC(1)
CRTTSDALC(1)
CTSDWRLHC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17482566</Reference>
<Target_Name>Paracetamol(4-acetamidophenol, 4AAP)</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>After 4 rounds of 4-AAP selection, 2-AAP and 3-AAP were used sequentially to delete those phages also binding to the structural isomers 2-AAP and 3-AAP from the 4-AAP binding pool.</Brief_Description>
<BiopanningDataSet_Comments>After 4 rounds of 4-AAP selection, 2-AAP and 3-AAP were used sequentially to delete those phages also binding to the structural isomers 2-AAP and 3-AAP from the 4-AAP binding pool. The identified NPNNLSH-phage clone displayed functional binding properties against paracetamol in solution, able in a peptide sequence-dependant manner to prevent the in vitro hepatotoxicity of paracetamol and reduce (~20%) the permeability of paracetamol across a semi-permeable membrane.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>419</BiopanningDataSetID>
<Peptides>CGPSEPIGAWDC
CGPAEPRGAWVC
CGPREPDGSWHC
CGPVEPVGAWVC
CGPWEPSGIWSC
CGPVEPKGVWFC
CGPYEPRGDWTC</Peptides>
<Motif>G-P-x-E-P-x(3)-W</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:18184085</Reference>
<Target_Name>Anti-CD4 monoclonal antibody 5145A</Target_Name>
<Template_Name>T-cell surface glycoprotein CD4</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>The human monoclonal antibody 5145A against HIV-1 gp120 was isolated from an asymptomatic, seropositive hemophiliac. The epitope of this HuMAb overlaps the CD4-binding site of gp120. The antisera from mimotope fusion protein immunized rabbit did not compete with CD4 for binding to gp120, although 5145A is specific for the conserved CD4 binding site region of the HIV envelope protein gp120. Perhaps, the template is not CD4.</Brief_Description>
<BiopanningDataSet_Comments>GPYEPRGDWT and GPAEPRGAWV bearing phage clones had the highest apparent affinity, whereas GPSEPIGAWD-phage 2 had the lowest. Rabbits immunized with peptide-protein fusions produced antisera that bound to recombinant HIV-1 gp120, but did not bind to HIV-infected cells nor neutralize HIV. The antisera also did not compete with CD4 or antibodies to the CD4 binding site for binding to gp120.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>420</BiopanningDataSetID>
<Peptides>YGLTALDPLFKP(4)
AFAKPLASDPLF(2)
KVLTAVDPLYYA(1)
KPLAMDPLHVST(1)
KPLASDPLGAMP(1)
KLSATDPLAHYK(1)
NLYAVDMLVLAR(1)
VTADMASDMLHH(1)
HIRLQAIDPMPP(1)
HLGLMAMDHLPW(1)
QTILAHDPVKMR(1)
HPLASSPLFAAP(1)</Peptides>
<Motif>A-x-D-[PM]-L</Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17504878</Reference>
<Target_Name>Anti-A. paragallinarum strain 0083 polyclonal antibody</Target_Name>
<Template_Name>Avibacterium paragallinarum strain 0083 (serovar 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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The phage clones containing the peptide motif reacted with the target antibody and this interaction could be blocked, in a dose-dependent manner, by A. paragallinarum. Immunization with YGLLAVDPLFKP-expressing recombinant bacteria induced a specific serological response to serovar A. A. paragallinarum. The chickens given the recombinant E. coli showed significant protection against challenge with A. paragallinarum 0083.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>421</BiopanningDataSetID>
<Peptides>CRDALGMIGQC(2)
CRNRLGMIQQC(2)
CRDGRGMMTQC(1)
CRDSTGMMAQC(1)
CRDSTGMVKQC(1)
CRDSAGMVGMC(1)
CRRRDGLIAQC(1)
CRGLEGDIVYC(1)
CRIRGGMGFAC(1)
CVRMSDTMLYC(1)</Peptides>
<Motif>R-[DN]-x(2)-G-[ML]-[VI]-x-Q</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:18716770</Reference>
<Target_Name>Matrix metalloproteinase-9, MMP-9</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>Recombinant human MMP-9 was immoblized through MMP-9 monoclonal antibody.
 0.01% arabinose was used during phage production.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>422</BiopanningDataSetID>
<Peptides>CRNRLGMIQQC(2)
CRDSEGNVTSC(1)
CRDSRGLVTQC(1)
CRDSYGSVAQC(1)
CRDNAGLVRQC(1)
CRDKEGNIASC(1)
CRNKAGLVTQC(1)
CMRNGQVFMVC(1)
CEPHSMRPC(1)</Peptides>
<Motif>R-[DN]-x(2)-G-[ML]-[VI]-x-Q</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:18716770</Reference>
<Target_Name>Matrix metalloproteinase-9, MMP-9</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>Recombinant human MMP-9 was immoblized through MMP-9 monoclonal antibody.
 0.01% arabinose was used during phage production.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>423</BiopanningDataSetID>
<Peptides>CRNDSGLVVQC(1)
CRNQFGTRVIC(1)
CRQRNGSVIQC(1)
CRTTTGEVAQC(1)
CMRLPSGFIHC(1)
CNYALKHKWFC(1)
CRDSTGMVKQC(1)</Peptides>
<Motif>R-[DN]-x(2)-G-[ML]-[VI]-x-Q</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:18716770</Reference>
<Target_Name>Matrix metalloproteinase-9, MMP-9</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>Recombinant human MMP-9 was immoblized through MMP-9 monoclonal antibody. 0.001% arabinose was used during phage production.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>424</BiopanningDataSetID>
<Peptides>CRDREGNVMRC(2)
CDVSQWGEALC(1)
CDVEQWGKAVC(1)
CRDASGMVDLC(1)
CRNELGMVAQC(1)
CRDREGLVRQC(1)
CRSREGDVMKC(1)
CRNGVGLVIQC(1)</Peptides>
<Motif>R-[DN]-x(2)-G-[ML]-[VI]-x-Q</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18716770</Reference>
<Target_Name>Matrix metalloproteinase-9, MMP-9</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>Recombinant human MMP-9 was immoblized through MMP-9 monoclonal antibody. 0.001% arabinose was used during phage production.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>425</BiopanningDataSetID>
<Peptides>HCWHYKFC(16)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18591232</Reference>
<Target_Name>serine repeat antigen 5, SERA5</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>X8 and CX8C phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Recombinant SERA5 enzyme domain was used for panning.</Brief_Description>
<BiopanningDataSet_Comments>Following six rounds of panning, 48 individual clones from the pool were propagated and tested for the ability to bind to SERA5. All of the clones from the 8-residue library were positive and displayed essentially no binding to the blocking protein. From these positive clones, 16 from the library pool were selected and sequenced.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>