<result><BiopanningDataSet><Item><BiopanningDataSetID>651</BiopanningDataSetID>
<Peptides>AHGYWEL(10)</Peptides>
<Motif>AHGYWEL</Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:19923010</Reference>
<Target_Name>Anti-chicken IL-2 monoclonal antibody 4F3</Target_Name>
<Template_Name>Interleukin 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.-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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>652</BiopanningDataSetID>
<Peptides>HHGYWEL(10)</Peptides>
<Motif>HHGYWEL</Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:19923010</Reference>
<Target_Name>Anti-chicken IL-2 monoclonal antibody 6H10</Target_Name>
<Template_Name>Interleukin 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.-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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>653</BiopanningDataSetID>
<Peptides>HGEVPRFHAVHL(14)
APWHLSSQYSRT(3)
DLNYFTLSSKRE(3)
SPLITSTLIPQR(2)
TALATSSTYDPH(2)
NRQSNWPIHKTI(1)
QLSEECSYLISRP(1)
QLTKNVPTYKSS(1)
SNPQPYTILPPV(1)
SPNQPYTILPPV(1)
TPLTLRTQTLTQ(1)
TTKQPHFHQKTL(1)
TTLVSTGQRTHP(1)</Peptides>
<Motif></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:20067240</Reference>
<Target_Name>Human embryonic stem cell line H9</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 library converged at the third round of screening, and 4-5 peptides dominated the sequence pool. A comparison of the number of unique sequences at each screening step revealed that convergence (such as HGEVPRFHAVHL) occurred not at the panning step but rather during amplification. Binding test was not done. </Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>654</BiopanningDataSetID>
<Peptides>SNHPATLTGTG(7)
TSPAYQATSPAP(5)
APWHLSSQYSRT(5)
SSLPPQQPSVSR(3)
SLPKFSDLLPRP(2)
ATQEIHASSALL(2)
LSTHTTESRSMV(2)
MPHLRSPSQDER(1)
QSDSDDLTVFAL(1)
QSQHTDPQYLYL(1)
SISKTSHSHTQY(1)
VQQKSSMVGPLL(1)</Peptides>
<Motif></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:20067240</Reference>
<Target_Name>Human embryonic stem cell line H9</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 library converged at the third round of screening, and 4-5 peptides dominated the sequence pool. A comparison of the number of unique sequences at each screening step revealed that convergence (such as SNHPATLTGTG, APWHLSSQYSRT and SSLPPQQPSVSR) occurred not at the panning step but rather during amplification. Binding test was not done.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>655</BiopanningDataSetID>
<Peptides>LTTAPKLPKVTR(1)
QLGTQPNSRTYA(1)
SRYITTMTNEQV(1)
TVKHRPDALHPQ(1)
LSTIGMPKLLA(1)
VTSRTIIPQGSA(1)
FAKSPDVSLNPS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:20067240</Reference>
<Target_Name>Human embryo carcinoma cell line NCCIT</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>phage display (biopanning and rapid analysis for selective interactive ligands, BRASIL panning, amplification-free panning)</Brief_Description>
<BiopanningDataSet_Comments>From 370 clones tested, seven cell-binding phage clones were identified and sequenced. Of the seven phage-derived peptides identified, all supported cell binding except FAKSPDVSLNPS. The self-assembled monolayers presenting LTTAPKLPKVTR were especially effective, as they supported cell adhesion over the broadest range of densities.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>656</BiopanningDataSetID>
<Peptides>ETTKLQRFQAML(50)
DHTLFAASHNHR(6)
DHTLFSTGHSHG(2)
DHTFMQRYHTHQ(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:20177903</Reference>
<Target_Name>Anti-TSOL18 monoclonal antibody 17E1</Target_Name>
<Template_Name>Activated oncosphere TSOL18</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>657</BiopanningDataSetID>
<Peptides>DTPYDLTG(15)
DTDSHVNL(9)
ERAPLSVE(6)
GDNSHVNL(5)
VGQDSDYS(4)
VSDNTDYS(3)
GPDSTWAG(2)
EGMMYTDV(2)
DLTYVNSQ(2)
DSSNKPTG(1)
DSSRLERV(1)
AHALTTEE(1)
APLPTNGE(1)
ATDHAAPQ(1)
ATPTTPDP(1)
EKFASNST(1)
EVSMYTDV(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>17</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20185523</Reference>
<Target_Name>Prostate carcinoma cell line PC3</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>f8-8mer phage display library (X8)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The naive library was sequentially exposed to culture flasks, serum treated culture flasks and non-target cells (fibroblasts) before being incubated with target PC3 cells. The sequenced phage clones were from eluate, post-elution wash and lysate.</Brief_Description>
<BiopanningDataSet_Comments>DTDSHVNL and DTPYDLTG demonstrated specificity and selectivity to PC3 cells based on target-association assays, microscopy and flow cytometry.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>658</BiopanningDataSetID>
<Peptides>DVVYALSDD(14)
AEYGESVNA(12)
AEYGERGNA(6)
AEYGESGNA(5)
EGLVWIGMD(3)
EAAGANIAP(2)
AEYGESVLI(1)
GAYDVNVND(1)
DSDVGWVND(1)
GPNWAEGDS(1)
VADDRDYSD(1)
VDVSEQMSL(1)
VGDNVDYMD(1)
VGDYDVVDS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20185523</Reference>
<Target_Name>Prostate carcinoma cell line PC3</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>f8-9mer phage display library (X9)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The naive library was sequentially exposed to culture flasks, serum treated culture flasks and non-target cells (fibroblasts) before being incubated with target PC3 cells. The sequenced phage clones were from eluate, post-elution wash and lysate.</Brief_Description>
<BiopanningDataSet_Comments>DVVYALSDD demonstrated specificity and selectivity to PC3 cells based on target-association assays, microscopy and flow cytometry.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>659</BiopanningDataSetID>
<Peptides>VQASNSN(39)
IPTHIRP(6)
LPPPPNP(3)
SPYRSLS(1)
SQTPKSK(1)
NQHTRVS(1)
LPLTPLP(1)
AVNSLQW(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19481546</Reference>
<Target_Name>Heart of the normotensive Wistar Kyoto rat (WKY)</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></Brief_Description>
<BiopanningDataSet_Comments>In the WKY rat, the heart-homing capabilities of phage displaying VQASNSN, SPYRSLS and IPTHIRP were much higher than those of insertless phage. For example, IPTHIRP phage was 49.8-fold higher.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>660</BiopanningDataSetID>
<Peptides>VQASNSN(60)
LPLTPLP(31)
DDTRHWG(9)
LPPPPNP(4)
IPTHIRP(3)
AVNSLQW(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19481546</Reference>
<Target_Name>Heart of the stroke prone spontaneously hypertensive rat (SHRSP)</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></Brief_Description>
<BiopanningDataSet_Comments>In the SHRSP rat, the heart-homing capabilities of phage displaying DDTRHWG and VQASNSN peptides were compared to insertless phage. VQASNSN homed to the heart at levels 200-fold higher than insertless phage. In addition, VQASNSN also homed to the lung, liver and kidney at levels more than 10-fold higher than insertless phage. DDTRHWG showed 46-fold enhancement in SHRSP rat compared to 11-fold in WKY rat further supporting its potential selectivity for the SHRSP heart.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>661</BiopanningDataSetID>
<Peptides>YDPWTPS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19624458</Reference>
<Target_Name>von Willebrand factor, vWF</Target_Name>
<Template_Name>Type I collagen</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>After three rounds of biopanning on a VWF-coated surface, 94 individual phage clones were grown, of which 10 bound to VWF. Eight clones displayed the same YDPWTPS peptide. Phages diplaying YDPWTPS bound to VWF in a specific and a dose dependent manner and specifically inhibited the VWF-collagen interaction under both static and flow conditions. YDPWTPS is the first peptide antagonist that binds to the VWF C domain and inhibits the VWF binding to collagen, suppressing platelet adhesion and aggregation under high shear conditions.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>662</BiopanningDataSetID>
<Peptides>CFQHPSFIC(7)
CSGYPRHYC(3)
CRQSHLKVC(2)
CKYNTHHAC(2)
CTGSPELHC(1)
CILGRIFSC(1)
CNQHTALSC(1)
CQMPEMKAC(1)
CWPNLTKEC(1)
CTVSTSIRC(1)
CPASKTLTC(1)
CLPSSGAAC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20186460</Reference>
<Target_Name>Lipopolysaccharide (LPS)-activated alveolar macrophages (AMs)</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>A strategy of sequential screening was applied by firstly binding the phage library to unmanipulated AMs and then binding the flow-through phages to LPS-activated AMs.</Brief_Description>
<BiopanningDataSet_Comments>After 4 rounds of panning, 22 out of 40 phage clones selected randomly bound selectively to LPS-activated AMs. The FQHPSFI peptide significantly inhibited LPS-stimulated microphage inflammatory protein 2 production in vitro.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>663</BiopanningDataSetID>
<Peptides>YSLRADSRWMPS(8)
KMDRHDPSPALL(4)
FQPHMARKLPSL(4)
TMAKSHMILEMA(1)
GDASIRNQMWLF(1)
TSNQNMTRLPPA(1)
TMGFTAPRFPHY(1)</Peptides>
<Motif>S-x(2)-T-M-x-R-x(2)-P-S-L</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20230853</Reference>
<Target_Name>Interleukin 2</Target_Name>
<Template_Name>IL-2 alpha receptor</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 phages were eluted with chicken CD25.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>664</BiopanningDataSetID>
<Peptides>TPDCTRWWCPLT(9)
TTCNNWVCFFEW(3)
MCTGKICWLNEM(3)
HTACSKTLCPLP(3)
VPHCSDTVCSLP(2)</Peptides>
<Motif>P-x-C-T-x-W-x-C-P-L-P</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20230853</Reference>
<Target_Name>IL-2 alpha receptor</Target_Name>
<Template_Name>Interleukin 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>The phages were eluted with chicken IL-2.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>665</BiopanningDataSetID>
<Peptides>LLADTTHHRPWT(0.5)
SVSVGMKPSPRP(0.1)
LLADTTHHRPWP(0.083)
LLADATHHSPWP(0.083)
HSVSNIRPMFPS(0.042)
SVSEGTHPSPRP(0.042)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20232090</Reference>
<Target_Name>Bevacizumab-treated tumor vasculature in nude mice</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>Cancer therapy response to was bevacizumab evaluated in LS174T human colorectal cancer model, which was made on the right shoulder of female athymic nude mice.</Brief_Description>
<BiopanningDataSet_Comments>LLADTTHHRPWT was found to be dominantly enriched in the bevacizumab-treated tumors.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>666</BiopanningDataSetID>
<Peptides>TNPNRRNRTPQMLKR(5)</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:18472186</Reference>
<Target_Name>Beta-amyloid protein 42</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>Subtractive steps were used to remove phages binding to streptavidin or rat Aβ. Thus, it can be used to select peptides that target the active site of human Aβ’s SOD like activity, a site not present in the highly homologous rodent sequence.</Brief_Description>
<BiopanningDataSet_Comments>Twenty individual phage clones were randomly picked and sequenced. However, only one sequence was given in the original paper. TNPNRRNRTPQMLKR significantly reduced Aβ42\'s SOD-like activity. This 15-mer peptide reduced Aβ42 neurotoxicity in a dose-dependent manner. Furthermore, comparative analysis of the 15-mer peptide with Clioquinol, a known inhibitor of Aβ’s metal-mediated redox activity, showed the 15-mer peptide to be equipotent to this metal chelator, under the same experimental conditions.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>667</BiopanningDataSetID>
<Peptides>PLPQML(8)
MTMPTM(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18472186</Reference>
<Target_Name>Beta-amyloid protein 42</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>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Subtractive steps were used to remove phages binding to streptavidin or rat Aβ. Thus, it can be used to select peptides that target the active site of human Aβ’s SOD like activity, a site not present in the highly homologous rodent sequence.</Brief_Description>
<BiopanningDataSet_Comments>Twenty individual phage clones were randomly picked and sequenced. However, only two sequences were given in the original paper. PLPQML significantly reduced Aβ42\'s SOD-like activity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>668</BiopanningDataSetID>
<Peptides>STPNPLPRWLVP(4)
ESSWQDMLYLLR(3)
WKTQTHPFWDDL(2)
QHTPHPLPPFLI(1)
SHKQDPLPWPRF(1)
KVQLPLPYPFPF(1)
KHDPLPYPHFLL(1)
HLWEHEMILDLL(1)
THRWQEELTLLL(1)
SGIHAYPHWLDH(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:19864424</Reference>
<Target_Name>Mitochondrial fission 1 protein</Target_Name>
<Template_Name>Dynamin-1-like protein</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>At the end of the third round of panning, plate binders were eliminated by binding to a BSA coated plate.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>669</BiopanningDataSetID>
<Peptides>FYSHSFHENWPS(26)
IKSNPQTSNEFL(1)
SAHGTSTGVPWP(1)
ELANSVPWASPP(1)
WSPGQQRLHNST(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:19891006</Reference>
<Target_Name>Troponin I, cardiac muscle</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>Thirty clones (20 from the 5th round and 10 from the 4th round) were sequenced. Kinetic indirect phage ELISAs revealed that FYSHSFHENWPS was found to have nanomolar affinities for for human troponin I while attached to the phage particles. However, the binding affinity was decreased by the presence of complex tissue culture media (MEM), and the addition of 10% calf serum further interfered with the binding of the target proteins. Coincidently, FYSHSFHENWPS was reported to be a BSA binder by SAROTUP.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>670</BiopanningDataSetID>
<Peptides>LANKHQRLHAAD(2)
FHSSWPVNGSTI(2)
STYFDPHGTHPQ(2)
HGDISQINSSPW(1)
DRAPLIPFASQH(1)
ASITHFKSGKSH(1)
TMGFTAPRFPHY(1)
NHVHRMHATPAY(1)
QHANHQAWNNLR(1)
WNRSPAFSGPYL(1)
HHEWTHHWPPPP(1)
TIPYHVPYKPPR(1)
HKTQTYPQAWMH(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:19891006</Reference>
<Target_Name>Troponin I, cardiac muscle</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>Of 54 clones sequenced at 4th or 5th round, 16 readable sequences were obtained. Kinetic indirect phage ELISAs revealed that FHSSWPVNGSTI was found to have nanomolar affinities for for human troponin I while attached to the phage particles. However, the binding affinity was decreased by the presence of complex tissue culture media (MEM), and the addition of 10% calf serum further interfered with the binding of the target proteins. Coincidently, FHSSWPVNGSTI was reported to be a plastic binder by SAROTUP.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>671</BiopanningDataSetID>
<Peptides>CKVALTLRC(5)
CLVYLTQRC(3)
CIVYLTQKC(3)
CKLAMTMKC(3)
CKVILTHRC(2)
CLWFPREQC(2)
CILYLTQKC(1)
CFLVMSQRC(1)
CMLPLYFPC(1)
CELPRSPSC(1)
CTVPAFPAC(1)
CTNSAMADC(1)
CKHEPTPNC(1)</Peptides>
<Motif>V-x-L-T-x-R</Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20156289</Reference>
<Target_Name>Tumor necrosis factor receptor superfamily member 10B</Target_Name>
<Template_Name>Tumor necrosis factor ligand superfamily member 10</Template_Name>
<Structure_of_Target_Template_Complex>1D0G,1D4V,1DU3,</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 target used is DR5-Fc, fusion of the ecto-domain of the receptor to the Fc-portion of human IgG1. Before the third round, a subtractive round was performed by incubating the amplified phage of round two with human IgG Fc fragment.</Brief_Description>
<BiopanningDataSet_Comments>After three rounds of biopanning against DR5, 25 clones were picked and sequenced. Only 14 clones showed binding to DR5 with ELISA. These DR5-binding clones correspond to the following sequences: CKVILTHRC, CKVALTLRC, CLVYLTQRC, CIVYLTQKC and CILYLTQKC. The synthesized peptide, YCKVILTHRCY, in both monomeric and dimeric forms, binds specifically to DR5 in such a way that TRAIL binding to DR5 is inhibited.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>672</BiopanningDataSetID>
<Peptides>CSPGGVVSVCIC(1)
CFSGCGWVVKWC(1)
CGERFPLVDPCC(1)
CSLRGLDLRCFC(1)
CWLPVVVGSRCC(1)
CVLGGLSVVFEC(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:20214576</Reference>
<Target_Name>Receptor tyrosine-protein kinase erbB-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>CX10C P99 β-lactamase-fusion library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The target used is the extracellular domain of ErbB2 receptor. Before panning, subtractive steps were taken with plastic and casein to remove non-specific binders.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>673</BiopanningDataSetID>
<Peptides>MCGVCLSAQRWT(1)
VSCPWLKYSGAL(1)
VWGLPSCTLAHG(1)
QSIFVDTMFRGS(1)
DDLSYLMVPGLL(1)
SGLWWLGVDILG(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:20214576</Reference>
<Target_Name>Receptor tyrosine-protein kinase erbB-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>X12 P99 β-lactamase-fusion library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The target used is the extracellular domain of ErbB2 receptor. Before panning, subtractive steps were taken with plastic and casein to remove non-specific binders.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>674</BiopanningDataSetID>
<Peptides>CGDGVWVGWVRC(2)
CGDRLCRMLWLC(1)
CGRVGMDVMGGC(1)
CGLGWCGVRWGC(1)
GGLHKDVCVAIF(1)
CMGWLPWWRTHC(1)
CPWLIRGLVGCC(1)
CGIRWLAFPYGC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20219829</Reference>
<Target_Name>Breast cancer cell line BT-474</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>CX10C P99 β-lactamase-fusion library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before panning, subtractive steps were taken with plastic and human non-cancer epithelial MCF 10A cells to remove non-specific binders.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>675</BiopanningDataSetID>
<Peptides>LSVCVRGLLGCG(2)
VCMNFVPAICRV(1)
KFLAYPSFFSRC(1)
LFMAGGSCYLSS(1)
DRCWSILATSTF(1)
HLLWVCPGGAPC(1)
VWGVFGGCSQRP(1)
LSVWMQGLSRSL(1)
VLGMARWVDLGS(1)
SVVSSVWRVSDS(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:20219829</Reference>
<Target_Name>Breast cancer cell line BT-474</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>X12 P99 β-lactamase-fusion library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before panning, subtractive steps were taken with plastic and human non-cancer epithelial MCF 10A cells to remove non-specific binders.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>