<result><BiopanningDataSet><Item><BiopanningDataSetID>426</BiopanningDataSetID>
<Peptides>SRAVCPVEVCRWVV(3)
FRAVCPPAVCYWHS(3)
EGWCEMHSRWCVVS(3)
SVYCEKFRWVCEFR(3)
LVCHPAVPALLCAR(1)
RCCAPYVPAFFCEC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</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>X14 and CX14C 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. Only approximately one-third of the clones from the 14-residue library pool were positive and displayed essentially no binding to the blocking protein. From these positive clones, 16 from the library pool were selected and sequenced. Addition of LVCHPAVPALLCAR to parasite cultures compromised development of late-stage parasites.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>427</BiopanningDataSetID>
<Peptides>CVSEDIYDAC(22)
CEFQQWSGKC(8)
CNHVCSRLGC(7)
CNETTVREYC(4)
CIEETARKGC(2)
CNELHMKQHC(2)
CNNATFEDGC(1)
CNNATVEDEC(1)
CEFLQWSGKC(1)
CETGERIVLC(1)
CDEKRGPNEC(1)
CHSWKPDKLC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18616802</Reference>
<Target_Name>Acute myeloid leukemia cells</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>Display PHAGE system library (CX6C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The peptides bound to leukemia cells, were internalized and could induce proliferation and/or differentiation in the target patient cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>428</BiopanningDataSetID>
<Peptides>CTNPESLTC
CKHHNWWTC
CSLRTYAAC
CFSSARLSC
CQRTTEANC
CTGYHNNTC
CSQWLQGS
CNSMWVRNC
CHTLPHTKC
CDLLLPGRC
CSTTNATWC
CHGSTKWAC
CYRTQFTQC
CTPLSTLQC
CTPGRSATC
CNPMHSRTC
CKPSTSGQC
CNKQFSAAC
CSPYAKHNC
CHSLRNAFC
CQGSPYRHC
CSAGAPEFC
CTQSGLLSC
CQVLNGNHC
CKSFTTTRC
CTYPYPKFC
CKSTFSPNC
CTSAAVHMC
CQPHLPWHC
CQTTNWNTC
CSASTESLC
CLVRNLAWC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>32</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18391034</Reference>
<Target_Name>Sin Nombre virus (SNV) strain SN77734</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>SNV was propagated and the titer was determined in Vero E6 cells. The preparation of UV-inactivated SNV was used for panning.</Brief_Description>
<BiopanningDataSet_Comments>The phages were eluted with anti-SNV IgG antibodies from human convalescent plasma (HCP). In all cases, the isolated peptides were less effective at blocking infection than were the same peptides presented by phage. Sin Nombre virus infection involves the interaction between viral membrane surface glycoproteins and the human integrin </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>429</BiopanningDataSetID>
<Peptides>CTTHISQTC
CHPSKALQC
CERLNLPQC
CTDNALKAC
CYKMDNHTC
CHVLDPHLC
CSRNHILTC
CVMSKHQHC
CLMGSSHSC
CPSHYTQAC
CHADQLPMC
CLPTPHHVC
CQLSLAPYC
CTFHSPRFC
CYATTLGAC
CGPSLRGVC
CFNTHTANC
CPGHHLSHC
CNSPKGKPC
CQWPGQSGC
CNSSSPTAC
CHQLMQNLC
CQATTARNC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>23</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18391034</Reference>
<Target_Name>Sin Nombre virus (SNV) strain SN77734</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>SNV was propagated and the titer was determined in Vero E6 cells. The preparation of UV-inactivated SNV was used for panning.</Brief_Description>
<BiopanningDataSet_Comments>The phages were eluted with polyclonal anti-Gn-BSA IgG. They were obtained sera from a rabbit immunized with the bovine serum albumin (BSA)-conjugated peptide LKIESSCNFDLHVPATTTQKYNQVDWTKKSS, which corresponds to residues 58 to 88 of Gn from SNV strain SN77734. In all cases, the isolated peptides were less effective at blocking infection than were the same peptides presented by phage. Sin Nombre virus infection involves the interaction between viral membrane surface glycoproteins and the human integrin αvβ3. Some peptides selected are similar to human integrin beta-3 (CD61: P05106).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>430</BiopanningDataSetID>
<Peptides>CLKDNHRSC(4)
CTPRQSPIC(4)
CYDPIWRTC(3)
CCYTAALAC(3)
CMLHAYAQC(2)
CFLGFSQQC(2)
CSVPINDSC(1)
CDHRQGSSC(1)
CAPYNTLAC(1)
CSPHIIASC(1)
CFSTNMKTC(1)
CRTTGAQTC(1)
CPLFKGMSC(1)
CLPAYSTYC(1)
CRDSSAHQC(1)
CHANFLHMC(1)
CSLNTRSQC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>17</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18670594</Reference>
<Target_Name>Cysteine-rich protein 1, CRP-1</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>CRIP1 was digested with enterokinase to remove the His tag and then used as target.</Brief_Description>
<BiopanningDataSet_Comments>LKDNHRS and YDPIWRT have the highest affinities for CRIP1. With peptide structure information and the NMR structure of CRIP1, the higher-affinity LKDNHRS was computationally redesigned, yielding a novel peptide, LDGGGKG, whose affinity was predicted to be much improved. Synthesis of this peptide and saturation and competitive binding studies demonstrated approximately a 10-28-fold improvement in the affinity of LDGGGKG compared to that of either LKDNHRS or YDPIWRTA1 peptide. VRPMPLQ does have partial homology (6 of 7 amino acids, V/LRPMPLQ) to the laminin-G domain of contactin-associated protein 1 (Caspr-1), which is present in human intestine and might be involved in contactin-mediated cell signaling and in tumor metastasis and invasion. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>431</BiopanningDataSetID>
<Peptides>VVFSTSV
ISARSSP
GDSMQQQ
LQVHTQN
WARSESP
AALVRHT
VRPMPLQ
NQPPDSY
APPWIAV
LPSSYPP
YTPLLPS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18345013</Reference>
<Target_Name>Fresh human colonic adenomas</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>Intact colon polyps freshly resected were used as the target.</Brief_Description>
<BiopanningDataSet_Comments>The binding of VRPMPLQ to HT-29 human adenocarcinoma derived cells was around 20-fold greater than its binding to Hs738.st/int nonmalignant human intestinal cells. The bindings of APPWIAV, LPSSYPP and YTPLLPS to HT-29 were similar to wild-type insertless M13 phages. The fluorescein-conjugated VRPMPLQ bound more strongly to dysplastic colonocytes than to adjacent normal cells with 81% sensitivity and 82% specificity. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>432</BiopanningDataSetID>
<Peptides>NAVWLPQHPLRT
SFHHLPIHPTAH
NPISSFYLPQHP
NSPWPLHPLRVF
YFPYPQHPTTSN
SLWLPWQPRHPP
KLIIGSPYPMHP
ANILAIHHPRHP
SLNLHLPLHPTF
VPHLPRHPLSSY
NPFLPRHPSPML
RLTLSPYPLHPL
SFHHLPIHPTAD
HPAHTMPRHPYT
TNYPWLPKHPTS</Peptides>
<Motif>L(0,1)-P-[QR]-H-P</Motif>
<Unique_Sequence_Number>15</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17847085</Reference>
<Target_Name>Anti-ErbB2 monoclonal antibody A21</Target_Name>
<Template_Name>Receptor tyrosine-protein kinase erbB-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></Brief_Description>
<BiopanningDataSet_Comments>Fifteen phage clones which showed the strongest reactivity to mAb A21 (ELISA signals &gt;1.0) and no crossreaction to another anti-ErbB2 mAb A18 were selected and sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>433</BiopanningDataSetID>
<Peptides>KLLRIAP(4)
ATWRIGP(4)
KTLRIAP(1)
KDVRIAP(1)
KVVRIEP(1)
NILSTLL(1)
NVFNWKW(1)
EFRWAWA(1)
DWTWSWN(1)
WSWGWMA(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:19081789</Reference>
<Target_Name>Anti-SHIV polyclonal antibody IgG</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.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The rhesus monkey was infected with SHIV-1157ip, an R5 SHIV strain encoding env of a recently transmitted Zambian HIV-C. Its polyclonal IgG was immobilized by a rabbit anti-monkey IgG and used as target. Eluted phages were subjected to negative selection using pooled sera from non-infected control monkeys.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>434</BiopanningDataSetID>
<Peptides>CSHGKLLAC(12)
CTGKLQCIC(3)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19081789</Reference>
<Target_Name>Anti-SHIV polyclonal antibody IgG</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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The rhesus monkey was infected with SHIV-1157ip, an R5 SHIV strain encoding env of a recently transmitted Zambian HIV-C. Its polyclonal IgG was immobilized by a rabbit anti-monkey IgG and used as target. Eluted phages were subjected to negative selection using pooled sera from non-infected control monkeys.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>435</BiopanningDataSetID>
<Peptides>GPSKIFTWGWAF(12)
IRPGPAAGGYPA(3)
SLWTLHGSLISA(3)
KMIHLGPQQTFP(2)
SLLYSSEYSGIW(2)
KLLSSNTYGIWM(2)
IRPHPGHMYYSW(1)
QVRMGPGQPDYL(1)
VRLPPGASGYTP(1)
KLLGYTTSAGIW(1)
LCYHRDGSYPTS(1)
SLLKHSLSAGIW(1)
QHSWSCSGKLLC(1)
SIWQTSGVLISY(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19081789</Reference>
<Target_Name>Anti-SHIV polyclonal antibody IgG</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 rhesus monkey was infected with SHIV-1157ip, an R5 SHIV strain encoding env of a recently transmitted Zambian HIV-C. Its polyclonal IgG was immobilized by a rabbit anti-monkey IgG and used as target. Eluted phages were subjected to negative selection using pooled sera from non-infected control monkeys.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>436</BiopanningDataSetID>
<Peptides>WSRPRSL(16)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:18309279</Reference>
<Target_Name>RNA-directed RNA polymerase NS5B</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>Twenty-six clones were sequenced. The binding of WSRPRSL to HCV NS5B in vivo was shown by a yeast two hybrid assay and by subcellular colocalization analysis using immunofluorescence confocal microscopy.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>437</BiopanningDataSetID>
<Peptides>TGPLPKE(8)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:18309279</Reference>
<Target_Name>RNA-directed RNA polymerase NS5B</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>Twenty-three clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>438</BiopanningDataSetID>
<Peptides>CATRLGRSSRC(18)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:18309279</Reference>
<Target_Name>RNA-directed RNA polymerase NS5B</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>CX9C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Twenty-six clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>439</BiopanningDataSetID>
<Peptides>CMAFFISRWRC(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:18309279</Reference>
<Target_Name>RNA-directed RNA polymerase NS5B</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>CX9C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Twenty-three clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>440</BiopanningDataSetID>
<Peptides>NYNLSRNLTWFY(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:18309279</Reference>
<Target_Name>RNA-directed RNA polymerase NS5B</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>Ten clones were sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>441</BiopanningDataSetID>
<Peptides>CKPTGMPQC(1)
CPTWALHLC(1)
CPTWLSPAC(1)
CRSPDMPFC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:18569284</Reference>
<Target_Name>Colon cancer cells</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>Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used.</Brief_Description>
<BiopanningDataSet_Comments>Twenty clones were sequenced. Samples of tumor and noncancerous colon tissue were obtained at the time of colectomy from patients with operable colon cancer. Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used. Initially, a subtraction step using non-cancerous colon tissue was performed. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>442</BiopanningDataSetID>
<Peptides>CSPIQDRHC(2)
CHMPTAQEC(1)
CKQYASPWC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:18569284</Reference>
<Target_Name>Colon cancer cells</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>Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used.</Brief_Description>
<BiopanningDataSet_Comments>Twenty clones were sequenced. Samples of tumor and noncancerous colon tissue were obtained at the time of colectomy from patients with operable colon cancer. Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used. Initially, a subtraction step using non-cancerous colon tissue was performed. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>443</BiopanningDataSetID>
<Peptides>CPTWLSPAC(2)
CPFSPSLKC(2)
CSPTKSNSC(2)
CQTTRSPIC(1)
CQHASPTNC(1)
CQPTPRSTC(1)
CPTPNHDHC(1)
CPTSHRNSC(1)
CPTTKLSTC(1)
CSIHGPTRC(1)</Peptides>
<Motif>SPT</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:18569284</Reference>
<Target_Name>Colon cancer cells</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>Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used.</Brief_Description>
<BiopanningDataSet_Comments>Thirty-seven clones were sequenced. Samples of tumor and noncancerous colon tissue were obtained at the time of colectomy from patients with operable colon cancer. Laser capture microdissection (LCM) is performed to separate only cancer cells as the target used. Initially, a subtraction step using non-cancerous colon tissue was performed. Phage clones displaying the SPT motif demonstrated 9-fold higher binding to colon cancer cells derived from a patient than insertless phage, while, recovery of the SPT phage from the colon cancer cell lines DLD-1 and HCT-15 was 7-fold higher than that of the control insertless phage. The binding of SPT phage to colon cancer cells from the patient was confirmed by immunofluorescence. Additionally, peptide SPTKSNS showed binding activity in the absence of mitogenic effects on colon cancer cells in vitro.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>444</BiopanningDataSetID>
<Peptides>TTFYRRGA
EASYRRKQ
ASSYRTSR
AAWYRTSR
ARLYSRGA
EAFYSQRF
TRFYSRGR
SFHYRMVG
GTLFRSGN
PNRWSTGA
SSEWSMPY
SSYISNFG
LEARSAYH
NAARSTGA
EAKRSYHS
EASRSATL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18359858</Reference>
<Target_Name>Kallikrein-1</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>fUSE55-based X8 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>From the third to the last round of screening, phage clones were randomly selected and plasmid DNA were isolated and sequenced to determine the displayed substrate peptide sequences. A total of six rounds of enrichment were performed for KLK1.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>445</BiopanningDataSetID>
<Peptides>EAVRSAMW
HLVRSWNG
VGVRSVYG
ASVRSAMY
SKVRSAGA
QMYRSSWG
FGFRSVHG
TAFRSAYG
TAFRNSLG
IGFRNAGA
SLFRMVVL
EAFRSSDQ
ASSRSVKW
AKSRSAGD
AFLRMASL
KVLRSATG
YMTRSAMG
ISTRSAIW
WGWRYAET
KEARSAYG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18359858</Reference>
<Target_Name>Kallikrein-6</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>fUSE55-based X8 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>From the third to the last round of screening, phage clones were randomly selected and plasmid DNA were isolated and sequenced to determine the displayed substrate peptide sequences. A total of five rounds of enrichment were performed for KLK6.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>446</BiopanningDataSetID>
<Peptides>CPHMTAPFC
CAPYSRFQC
CQPPDRPMC
CPDHERPMC
CPLREHPMC</Peptides>
<Motif>RPMP</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:18583245</Reference>
<Target_Name>Large intestinal cancer cell line LoVo</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 normal large intestinal mucosal epithelial cells were used to remove non-specific phages to LoVo cells.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>447</BiopanningDataSetID>
<Peptides>SPWSEPAYTLAP
APWTEHSYYLSL
VTHKTCPPACWP</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:18782762</Reference>
<Target_Name>Claudin-4</Target_Name>
<Template_Name>Heat-labile enterotoxin B chain</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>CHO cells transfected with full-length Cldn-4 (CHO-Cldn-4) were used as the target. CHO control cells were used to remove phage specific for CHO determinants in the 2nd and the 4th round.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>448</BiopanningDataSetID>
<Peptides>SFSIIHTPILPL(1)
ELMNPLLPFIQP(1)
HLPSTGNQYLSL(1)
ETNWTHRPPLRV(1)
EYRMAHLTPSLL(1)
YHLQDSETLSLL(1)
SPWYMTPSPNTA(1)
SVSVGMKPSPRP(1)
DPMTWTPSSVMR(1)
TPHRLDWSPHLV(1)
GSNPWNTWLTTL(1)
NPFNQHLHAQHP(1)
SESKDPTLWYPA(1)
SFRLATPESSRV(1)
SNNEPMLRYTGQ(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>15</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18347144</Reference>
<Target_Name>Hepatocellular carcinoma line Mahlavu</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>Ninety-six phage clones were randomly isolated and used to react with hepatocellular carcinoma cells and normal epithelial cells by ELISA assay. Fifteen phage clones with higher hepatocellular carcinoma cell reactivity by ELISA and flow cytometry were selected and sequenced. In vivo, SFSIIHTPILPL phage homed specifically to tumor tissues but not to normal visceral organs in severe combined immunodeficient mice bearing human hepatocellular carcinoma xenografts. This homing ability could be competitively inhibited by synthetic peptide, SFSIIHTPILPL. Immunohistochemical staining confirmed that SFSIIHTPILPL phage localized to tumor tissues and that it could not be detected in SFSIIHTPILPL-competed tumor tissues. In addition, SFSIIHTPILPL phage recognized the tumor tissue but not nontumor tissue in surgical specimens from hepatocellular carcinoma patients, with a positive rate of 61.3% (19 of 31). With the conjugation of SFSIIHTPILPL and liposomal doxorubicin, the targeted drug delivery system enhanced the therapeutic efficacy against hepatocellular carcinoma xenografts through enhanced tumor apoptosis and decreased tumor angiogenesis. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>449</BiopanningDataSetID>
<Peptides>QRFCTGHFGGLYPCNGP(23)
GGGCVTGHFGGIYCNYQ(4)
KIICSPGHFGGMYCQGK(3)
PSYCIEGHIDGIYCFNA(3)
NSFCRGRPGHEGGCYLF(1)</Peptides>
<Motif>G-H-F-G(2)-x-Y</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:18272495</Reference>
<Target_Name>HEK293 cells transfected with hFcRn and hβ2m (293c11)</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>3M17,3M1B,</Structure_of_Target_Peptide_Complex>
<Library_Name>TN phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In the motif, X is preferably a hydrophobic amino acid. The pooled phage libraries were screened with HEK293 cells transfected with hFcRn and hβ2m (293c11) by using competition with hIgG to select for phage capable of interfering with the IgG–FcRn interaction at pH 6. The subtraction step was performed twice by incubating the phage with the untransfected 293 cells.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>450</BiopanningDataSetID>
<Peptides>CAYHRLRRC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2-4</Rounds_of_Panning>
<Reference>PMID:18292083</Reference>
<Target_Name>Acute T-lymphoblastic leukemia Molt-4 cells</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>fUSE5-based CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Ninety-six clones were sequenced after the second, third, and fourth round of panning. There were 1, 17 and 55 clones respectively had the sequence CAYHRLRRC. CAYHRLRRC contains a lymph node-homing motif (CAY) and a cell-penetrating motif (RLRR). Binding of this ligand-directed phage to a large panel of leukemia/lymphoma cells and to patient-derived samples was much higher than to non-leukemia control cells. </BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>