<result><BiopanningDataSet><Item><BiopanningDataSetID>1326</BiopanningDataSetID>
<Peptides>HEIGSLAGLAMR(1)
AHFNGSLRSLTQ(1)
IINTGSLLSLAH(1)
DTGSLVWLSQRS(1)
HNHGSISALMHL(1)
DHDRLIRRTAQI(1)
FHTLDNNIRNVN(1)
FHDTSLLSHHLA(1)</Peptides>
<Motif>G-S-L-x(2)-L</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:20961714</Reference>
<Target_Name>Anti-FMDV Asia1 antigen monoclonal antibody 3E11</Target_Name>
<Template_Name>Polyprotein</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>Through a 12-mer random peptide phage display, synthetic peptide analysis and constructing a series of FMDV Asia1/YS/CHA/05 mutants using reverse genetic system, we finely mapped the neutralizing epitope as the 12-amino acid peptide 141SXRGXLXXLXRR152.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1327</BiopanningDataSetID>
<Peptides>ELKQSAQVQAKI
HLWSFALPSAQV
INSARIMPPNWR
TSPQARLEAIEP
YSLRQDYNPEPV
YSLRQDVLVLEE
YSLRNDWPTLPP
SLTNSMFPGYAY
HMSIWPERWPLS
HSLRPEWRMPGP
FQIAPTDPASNA
SPKIISSGLPTY
TSSGLAPTPIMQ
FGTGLASHSPAW
HNLVPRHLGTVL
SYQWHHLGTWLT
STYGSHLGWGHF
GIHLNFKVTHMH
WHSTMSWTNSTW
AGHDRLAVTPSS
LTRSLDSHSMNT</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>21</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21071249</Reference>
<Target_Name>Methylmalonic aciduria and homocystinuria type C protein</Target_Name>
<Template_Name>Methylmalonic aciduria and homocystinuria type D protein, mitochondrial</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 MMACHC-affinity-selected peptides were scanned against MMADHC to predict binding sites of MMACHC on this protein. Five distinct regions of multiply-aligning clusters were located along the primary sequence of MMADHC. Two regions were positioned in a domain with homology to ATPase component of a bacterial ATP-binding cassette (ABC) transporter: Region I, residues142-150; and Region II, residues 157-169. The other three regions were located in the C-terminal domain of MMADHC: Region III, residues 220-236; Region IV, residues 246-256; and Region V, residues 280-290.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1328</BiopanningDataSetID>
<Peptides>LLDSARH
GPASGPM
TPSSNRF
AHTPNSR</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:21071249</Reference>
<Target_Name>Methylmalonic aciduria and homocystinuria type C protein</Target_Name>
<Template_Name>Methylmalonic aciduria and homocystinuria type D protein, mitochondrial</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></Brief_Description>
<BiopanningDataSet_Comments>The MMACHC-affinity-selected peptides were scanned against MMADHC to predict binding sites of MMACHC on this protein. Five distinct regions of multiply-aligning clusters were located along the primary sequence of MMADHC. Two regions were positioned in a domain with homology to ATPase component of a bacterial ATP-binding cassette (ABC) transporter: Region I, residues142-150; and Region II, residues 157-169. The other three regions were located in the C-terminal domain of MMADHC: Region III, residues 220-236; Region IV, residues 246-256; and Region V, residues 280-290.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1329</BiopanningDataSetID>
<Peptides>NMNKHPLAYTEP(1)
FHWSWYTPSRPS(5)
WHFEWWRATPSG(1)
VLPPKPMRQPVA(1)
HLQSMKPRTHVL(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:21214859</Reference>
<Target_Name>Glutathione S-transferase, GST</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></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1330</BiopanningDataSetID>
<Peptides>CHLYTAGSCNMS(2)
CHLSATGACRMI(5)
IGSDMKGMPKPR(1)
KSLSRHDHIHHH(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21214859</Reference>
<Target_Name>Cytoplasmic domain of CORYNE</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>In fact, the target is recombinant glutathione S-transferase(GST)-CRN-His6.</Brief_Description>
<BiopanningDataSet_Comments>Two positive clones that specifically bind to the intracellular protein kinase domain of CRN, CHLYTAGSCNMS and CHLSATGACRMI, have been identified. Alignment of these peptides and the kinase-associated protein phosphatase (KAPP) shows high similarity, indicating that KAPP might interact with the cytoplasmic kinase domain of CRN and negatively regulate the CLV signal.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1331</BiopanningDataSetID>
<Peptides>SYTFHWHQSWSS(3)
QSWSWHWTSHVT(3)
WTWRWAHVTNTR(1)
QDVHLTQQSRYT(1)
HKAHEYDPWISP(1)
SYSQHYGIPNPW(1)
SSWQMSWSWMGS(1)</Peptides>
<Motif>QSWS</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:21259034</Reference>
<Target_Name>Dry degummed silk fibroin fibers</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></Brief_Description>
<BiopanningDataSet_Comments>The selected silk-binding peptides contained a consensus sequence QSWS which is important for silk-binding as confirmed by binding assays using phage and synthetic peptides.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1332</BiopanningDataSetID>
<Peptides>EHYLDKWASHDM(1)
LPQLNTLDKWAT(2)
ASSLDKWALYTS(2)
AAMTNHVLDKWA(1)
YKLDKWAPSLSK(1)
YPTLDKWAMWMH(1)
KHLALDKWSILA(1)
LPHLDKWSSITP(1)
ITPALDKWSTRF(1)
QVPLDKWSVAWP(1)
MDLDKWNMKSLT(1)
SLDKWVLAPLAY(1)
NGLDISLDKWGV(1)
HPLTLLDKWTLL(1)
QSHYDKWASWGF(1)
ALSEDKWASTAS(1)
YGFPYDKWASRP(1)
NMDKWAAVFQSK(2)
YLPDKWATPQMI(1)
ATNYDKWALPYT(1)
EHAYDKWAQRXX(1)
TPDKWALPHPTL(1)
QFIPDKWARSPN(1)
AIQLVYDKWAMP(1)
HLPYTSDKWALM(1)
YMDKWANIVALR(1)
SHPGPDKWQTLP(2)
TPDKWYGLAPYR(2)
TPDLWSYLSNLQ(1)
TNLFDKWSYLAS(1)
YPNIDKWVALYH(1)
ANDPDKWNLTPL(1)
SPIHDKWSDLSR(1)
TPFLDKWVALKP(1)
YLPTDKWSHLRT(1)
SWPFDKWSQSLS(1)
SLHETHMLDRWA(1)
TTLQTLDRWSQL(2)
LESSLDRWTTLA(2)
QTMDRWASLRWS(1)
LVPDRWAFLQMS(2)
MPDPDRWALWPL(1)
ALVSDRWSWMHQ(1)
ETLAKDRWVTLG(1)
DPWAFRWPSGPM(1)</Peptides>
<Motif>ELDKWAS</Motif>
<Unique_Sequence_Number>45</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21237206</Reference>
<Target_Name>Anti-HIV-1 gp41 MPER monoclonal antibody 2F5</Target_Name>
<Template_Name>HIV-1 gp41 membrane proximal exterior region (MPER)</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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1333</BiopanningDataSetID>
<Peptides>CKTLDKWAC(4)
CMALDKWAC(2)
CWHLDKWAC(2)
CWTLDKWAC(1)
CLVLDKWAC(1)
CLRLDKWAC(1)
CVSLDKWAC(1)
CLGNDKWAC(1)
CDKWAPPTC(5)
CDKWAGLLC(4)
CDKWAPTSC(3)
CDKWALAYC(2)
CDKWAPRSC(1)
CDKWAVRWC(1)
CDKWAPPSC(1)
CDKWAEQYC(1)
CDKWASQPC(1)
CDKWAFMTC(1)
CDKWAPPGC(1)
CDKWAPSAC(1)
CDKWAPSWC(1)
CDKWAQTYC(1)
CDKWATRFC(1)
CDKWAGRAC(1)
CDKWAGPRC(1)
CDKWAPRQC(1)
CDKWAIPWC(1)</Peptides>
<Motif>LDKWA</Motif>
<Unique_Sequence_Number>27</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21237206</Reference>
<Target_Name>Anti-HIV-1 gp41 MPER monoclonal antibody 2F5</Target_Name>
<Template_Name>HIV-1 gp41 membrane proximal exterior region (MPER)</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>1334</BiopanningDataSetID>
<Peptides>SNFFDRTWPKLT
YNFFDRTWPKLT
SHRQHETDRNWP
NYPEDFFQRTWP</Peptides>
<Motif>F(2)-D-R-T-W-P</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:21264311</Reference>
<Target_Name>Anti-DENV2 monoclonal antibody 2A10G6</Target_Name>
<Template_Name>Dengue virus 2, DENV2</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>After three rounds of panning, 94 positive phage clones were identified and subjected to DNA sequence analysis. The results showed that 86 of the positive clones displayed 12 amino acid residues in common, i.e., SNFFDRTWPKLT. Phage-display biopanning and structure modeling mapped 2A10G6 to a new epitope within the highly conserved flavivirus fusion loop peptide, the 98DRXW101 motif.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1335</BiopanningDataSetID>
<Peptides>APRDPLS(1)
DPFFYTP(1)
GLDHHPP(1)
GYDKHPQ(1)
HFTNHPQ(2)
HLANHPQ(1)
HLENHPM(2)
HLIAHPQ(1)
HLYAHPQ(2)
HRISWPS(1)
HYEGHPQ(1)
IAPNHPQ(2)
IPEWHPQ(8)
IPYWHPQ(3)
ISSTHPQ(1)
MQSHQDS(1)
NLISHPQ(1)
NLLNHPQ(11)
NLVNHPQ(4)
NLVSHPQ(1)
NPTKHQM(1)
PLLAHPQ(1)
SLIAHPQ(4)
SLLAHPH(1)
SLLAHPQ(7)
SLLSHPQ(2)
SLVSHPM(1)
SPTYQRL(1)
TLIAHPQ(1)
TLISHPQ(5)
TLLAHPQ(8)
TLLNHPQ(2)
TLQPGGA(1)
TPSPLAG(1)
VTPTMHP(1)
YLVNHPQ(1)
YMEHSRV(1)</Peptides>
<Motif>HPQ</Motif>
<Unique_Sequence_Number>37</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21278676</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5,</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></Brief_Description>
<BiopanningDataSet_Comments>One hundred phage isolates were sequenced after the fourth round of selection against streptavidin-coated beads.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1336</BiopanningDataSetID>
<Peptides>HHHPPLA(5)
HHPPFPP(2)
HPPSWGD(2)
HPPHFPN(1)
HPTGLFR(2)
HNHLGVH(2)
KPFHNST(5)
KPGYSSA(2)
KPPQVPL(2)
KPHAPHR(1)
KPPHHPR(3)
KPPHPVY(1)
KPVKVPR(2)</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:21278676</Reference>
<Target_Name>Unmodified helix 31 of bacterial 16S ribosomal RNA</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>Duplicate samples of unmodified h31 on magnetic beads were employed for selection. For each sample of unmodified h31, 100 isolates were sequenced. Two hundred phage isolates were sequenced after the fourth round of selection against unmodified h31 on streptavidin-coated beads. </Brief_Description>
<BiopanningDataSet_Comments>Two hundred phage isolates were sequenced after the fourth round of selection against unmodified h31 on streptavidin-coated beads. Only peptides with repeated sequences or common motifs are shown.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1337</BiopanningDataSetID>
<Peptides>FVRPFPL(6)
FVRPFAL(4)
FVRPYAP(2)
FPRTIAP(1)
DIRTQRE(4)
DIRTQTR(2)
DIRATQA(2)
ATPLWLK(5)
ATPTQRE(3)
ATPLYLR(2)
TLWDLIP(5)
TLWSFMP(3)
TLWVPSR(2)
TLTTLTN(2)
TLTFFHR(2)
TYLPWPA(5)
TYLPWPP(2)
TYLRARL(3)
TYPFAPW(2)</Peptides>
<Motif>TLW, VRP</Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21278676</Reference>
<Target_Name>Modified helix 31 of bacterial 16S ribosomal RNA</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>Duplicate samples of h31 on magnetic beads were employed for selection. For each sample of h31, 100 isolates were sequenced. Phage isolates were sequenced after the third round of selection against wild-type modified h31 on streptavidin-coated beads.</Brief_Description>
<BiopanningDataSet_Comments>Two hundred phage isolates were sequenced after the third round of selection against wild-type modified h31 on streptavidin-coated beads. Only peptide sequences with repeated sequences or common motifs are shown. Several of the peptides exhibited moderate affinity (in the high nM to low μM range) to modified helix 31 in biophysical assays, including surface plasmon resonance (SPR), and were also shown to bind 30S ribosomal subunits. These peptides also inhibited protein synthesis in cell-free translation assays.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1338</BiopanningDataSetID>
<Peptides>CVRPFAL(5)
CVRAPTL(2)
TVRPFTL(2)
TLWDLIP(2)
TLWPLSP(2)</Peptides>
<Motif>TLW, VRP</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:21278676</Reference>
<Target_Name>Modified helix 31 of bacterial 16S ribosomal RNA</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>A separate counter selection was also carried out in the third round of selection against wild-type h31 in which free unmodified h31 was added to the phage and modified h31-streptavidin mixture.</Brief_Description>
<BiopanningDataSet_Comments>One hundred phage isolates were sequenced after the third round of selection. Only peptide sequences with repeated sequences or common motifs are shown. Several of the peptides exhibited moderate affinity (in the high nM to low μM range) to modified helix 31 in biophysical assays, including surface plasmon resonance (SPR), and were also shown to bind 30S ribosomal subunits. These peptides also inhibited protein synthesis in cell-free translation assays.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1339</BiopanningDataSetID>
<Peptides>SDSLMKKPGGPG(1)
MYHHRKKPGGPG(1)
MGAMHKKPGKTG(1)
VHKYDKKRGKRG(1)
PTGKMKKAGGLL(1)
EPPRYKKHGGAS(1)
AHHTLLELWTQA(1)
ASYSNLTHWLSS(1)
SPRLTTYKASPK(1)
DMHHKPGRTLHH(1)</Peptides>
<Motif>K(2)-P-G(2)-P-G</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:21375771</Reference>
<Target_Name>Anti-WNV C protein monoclonal antibody 6D3</Target_Name>
<Template_Name>Capsid protein C</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 mAb 6D3 recognized the phages displaying a consensus motif consisting of the amino acid sequence KKPGGPG, which is identical to an amino acid sequence present in WNV C protein. Further fine mapping was conducted using truncated peptides expressed as MBP-fusion proteins.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1340</BiopanningDataSetID>
<Peptides>AYYPQNHKSNAE</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:21329494</Reference>
<Target_Name>Bovine serum albumin (BSA)</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></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1341</BiopanningDataSetID>
<Peptides>WHWRNPDFWYLK(0.225)
WHWTWLSEYPPP(0.215)
LETSKLPPPAFL(0.125)
WHWSQWLSGSPP(0.085)
WHRTPQFWAFPW(0.07)
SVSVGMKPSPRP(0.05)
WHKTPWFWPTNL(0.05)
WHWSWQPQRHSP(0.04)
WHWQYTPWWRGS(0.03)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:21329494</Reference>
<Target_Name>Gliadin</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>Panning was done both with gliadin dissolved in urea and in NaHCO 3. Since electrostatic binding of the phage to the target protein weakens with increasing ionic strength, which in turn influences the specificity of the interaction, different buffers with different ionic strengths were tested prior the actual panning experiments.</Brief_Description>
<BiopanningDataSet_Comments>Although identical sequences were frequently picked up in independent experiments, altogether more than 160 unique sequences encoding peptides with potential gliadin binding activities were identified. In order to confirm that the selected phage clones interacted with gliadin proteins, nine different phage populations that had repeatedly been picked up in different panning experiments were chosen. Together, these nine sequences represent 89% of all identified gliadin-binding sequences.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1342</BiopanningDataSetID>
<Peptides>HAPVQPN(1)
CTGPTSLSC(2)
CKPMQFVHC(1)
CSSYEYHAC(1)
CSTQAHPWC(1)
CGTSRLFSC(1)
CASHNPKLC(1)
CPAKQKAHC(2)
CSASGTPSC(1)
CTRFYRPSC(1)
CQNPRQIYC(4)
CNPQMQRSC(5)
CNYPTLKSC(7)
NPYHPTIPQSVH(4)
HQFISPEPFLIS(1)
SPNFSWLPLGTT(2)
SVSVGMKPSPRP(2)
TPLTSPSLVRPQ(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21291244</Reference>
<Target_Name>Single-crystal hydroxyapatite (HAP)</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, Ph.D.-7 and Ph.D.-C7C phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In last round, the HAP binding phages were simultaneously exposed to the HAP target substrate in solution.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1343</BiopanningDataSetID>
<Peptides>CNERQMELC(1)
CNKPLSTLC(1)
CHTLLSTTC(1)
CLKPFSGAC(1)
CLGPGKAFC(4)
CSTSAKHWC(1)
TMGFTAPRFPHY(7)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21291244</Reference>
<Target_Name>Polycrystalline hydroxyapatite (HAP)</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, Ph.D.-7 and Ph.D.-C7C phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In last round, the HAP binding phages were simultaneously exposed to the HAP target substrate in solution.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1344</BiopanningDataSetID>
<Peptides>HWKHLHNTKTFL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21295090</Reference>
<Target_Name>Amino acid (160)REVPYAYIREGHEKQ(174) of MMP-14</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></Brief_Description>
<BiopanningDataSet_Comments>Peptide HWKHLHNTKTFL (denoted as MT1-AF7p) showed high MT1-MMP binding affinity. Computer modeling verified that MT1-AF7p binds to the MT-loop region of MT1-MMP and interacts with MT1-MMP through hydrogen bonding and hydrophobic interactions.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1345</BiopanningDataSetID>
<Peptides>TYTDWLNFWAWP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:21297616</Reference>
<Target_Name>Myelin basic protein, MBP</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>In the selection against MBP, phage expressing a library of peptides were selected through multiple cycles for binding to biotinylated MBP, using avidin agarose to isolate selected phage. Specifically, the phage library was mixed with biotinylated MBP and allowed to bind for 1 h. Avidin agarose was added and incubated for an additional hour. Nonbinding phage were removed by washing the agarose three times with PBS solution and the supernatant was plated for titer and amplification for subsequent cycles.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1346</BiopanningDataSetID>
<Peptides>NTQTLAKAPEHT(5)
KSLSRHDHIHHH(2)
DFTKTSPLGIH(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:21297616</Reference>
<Target_Name>Excised murine peripheral nerves</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>Specifically, for positive selection using nerve tissue, nerve tissue was dissected/washed and mixed with a phage library. For negative selection using nonnerve tissues, nonnerve tissues (muscle and fat) were dissected from normal mice and incubated with the phage library obtained from the positive selection. </Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1347</BiopanningDataSetID>
<Peptides>AHHNSWKAKHHS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>8</Rounds_of_Panning>
<Reference>PMID:21297616</Reference>
<Target_Name>Nerve tissue (sciatic, brachial plexus, cranial nerves)</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></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1348</BiopanningDataSetID>
<Peptides>CSTSMLKAC(79)
CKPGTSSYC(20)
CPDRSVNNC(18)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21316369</Reference>
<Target_Name>Ischemic region of left ventricular (LV) </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 CSTSMLKAC sequence was capable of mediating selective homing of phage to ischemic heart tissue.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1349</BiopanningDataSetID>
<Peptides>CWEPMNHLC(14)
CPFASYLHC(13)
CENVWYPRC(9)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21316369</Reference>
<Target_Name>Non-ischemic region of left ventricular (LV) </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 first two rounds of bio-panning were performed against ischemic left  ventricular (LV) tissue.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1350</BiopanningDataSetID>
<Peptides>CQSTMSTLC(13)
CPTSFLTDC(9)
CYDLRSHQC(7)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21316369</Reference>
<Target_Name>Right ventricular (RV) </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 first two rounds of bio-panning were performed against ischemic left  ventricular (LV) tissue.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>