<result><BiopanningDataSet><Item><BiopanningDataSetID>351</BiopanningDataSetID>
<Peptides>CARGSSQSC
CASPGSSFC
CCAIGGAAC
CFYGAAELC
CGAASVKIC
CGAAYSALC
CGDRLLGPC
CGRWLLGGC
CGSSLRSLC
CGVGSSDRC
CIGGGGSSC
CIHGAAVYC
CLLGGQLSC
CLLGVGILC
CRGSSAWAC
CSVRSLLGC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:16581960</Reference>
<Target_Name>C57Bl/6 female mice uterus</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>352</BiopanningDataSetID>
<Peptides>CAAGVGVNC
CFAGVFVLC
CTRAGVVTC
CVAWRDSLC
CLWRDRAGC
CARDWRDYC
CFSWRDARC
CTSTFGGRC
CACFGGEGC
CVVLRFGGC
CERGWFGGC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:16581960</Reference>
<Target_Name>C57Bl/6 female mice bowel</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>353</BiopanningDataSetID>
<Peptides>VHPKQHR
TASNNNS
TISNKSQ
TYSNSYP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17000904</Reference>
<Target_Name>Vascular cell adhesion protein 1, V-CAM 1, VCAM-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.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>An M13 phage library was injected into the tail vein of cholesterol-fed apoE-/- mice. Internalized phages were retrieved from dissected aortic plaques and then reinjected into subsequent mice for a total of 3 rounds of positive selection.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>354</BiopanningDataSetID>
<Peptides>CVHSPNKKC[1.000]
CDHASPMHC[0.574]
CPTRIGQMC[0.141]
CMHRAHQMC[0.370]
CISHQMPAC[0.154]
CPGHHTSQC[0.272]
CNNAHHKNC[0.190]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:15653572</Reference>
<Target_Name>Vascular cell adhesion protein 1, V-CAM 1, VCAM-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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 650 nm was measured (Emax; Molecular Devices). Data, relative absorbance, were reproduced from the graph and shown.</Affinity_Measurement_Description>
<Brief_Description>Phage selection and negative depletion were performed using strain-matched murine cardiac endothelial cells (MCECs) and murine lung endothelial cells (MLECs).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>355</BiopanningDataSetID>
<Peptides>CSSSPSKHC(8)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:16565728</Reference>
<Target_Name>Mouse abdominal skin</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>356</BiopanningDataSetID>
<Peptides>SWLELRP(7)
EGWHAHT(5)
KLWTIKP(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12649290</Reference>
<Target_Name>V-type proton ATPase 116 kDa subunit a isoform 4</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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>357</BiopanningDataSetID>
<Peptides>WHLPFKC(6)
WHKPFRF(3)
HSLRTTF(1)
LPKRSPI(1)</Peptides>
<Motif>W-H-x-P-F-x(2)</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:17401149</Reference>
<Target_Name>Vascular endothelial growth factor A, VEGF-A</Target_Name>
<Template_Name>Vascular endothelial growth factor receptor 1, VEGFR-1</Template_Name>
<Structure_of_Target_Template_Complex>1FLT,1QTY,</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 recombinant human VEGF165 contained in bovine serum were used for screening. The template is likely to be VEGFR1; however, other possiblities exist.</Brief_Description>
<BiopanningDataSet_Comments>These peptides inhibit VEGF dependent human umbilical vein endothelial cell proliferation. Two selected peptides with sequences WHLPFKC and WHKPFRF bind the VEGF homodimer in a concentration-dependent manner, with micromolar affinity, and with a 2:1 peptide:VEGF stoichiometry. They inhibited HUVEC proliferation in vitro by 77 and 55%, respectively.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>358</BiopanningDataSetID>
<Peptides>CAGALCY(28)
CXRCTVLLACKL(2)
CAGALCYYRAKC(1)
CAGXAVTXGGK(1)
CAGXPGXAG(1)
CTGRMTXQXXXA(1)
CQGNKTVQNSVS(1)
CAATDHQPEAKCKLA(1)
CATQVQHEAMHC(1)
CTGXCDLXQR(1)
YDPXKQL(1)
CPAEXRAGPVTT(1)
CEKNPPTVXNY(1)
VTPGTVSLRPHS(1)
FTPRTIGHINWC(1)
CMVERKRDEARV(1)
LYMIKWPGSEDC(1)
CSXCMDXFWAFL(1)</Peptides>
<Motif>CAGALCY</Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:17377744</Reference>
<Target_Name>Mouse brain microvasculature</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 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For each round, purified phages in PBS were injected into mouse via the tail vein. One hour later, brains were harvested, rinsed with cold PBS and homogenized for titering and amplification. This way, phages binding to brain microvasculature were enriched. The template of the brain-specific peptide CAGALCYA is surpposed to be a receptor or ligand involved in cell adhesion to endothelium of the brain microvasculature. Screening in vivo has inherent issues of high background, all the more apparent when a high complexity library is administered. The authors suggest there is an upper limit of library diversity of one in 10e5 pfu, if a hit is to be reliably identified by in vivo phage display.</Brief_Description>
<BiopanningDataSet_Comments>X in the mimotope sequence denotes unknown residue. The brain-specific peptide CAGALCY inhibits platelet adhesion to endothelium in vivo.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>359</BiopanningDataSetID>
<Peptides>CFNGKDWLYC(9)</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:17973501</Reference>
<Target_Name>Phenoxibenzoic acid-polyclonal antibody complex</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>pAFF/MBP vector-based phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Antibodies specific for PBA, were purified on 3-((2-oxoethoxy)ethoxy)phenoxybenzoic acid coupled Sepharose, from serum of rabbits immunized with a hapten-KLH conjugate.</Brief_Description>
<BiopanningDataSet_Comments>The phage borne peptide did not bind to the analyte-KLH conjugate, which demonstrated that the peptide is specific for the PBA-antibody immuncomplex.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>360</BiopanningDataSetID>
<Peptides>QPWLEQAYYSTF
YPHIDSLGHWRR
LLADTTHHRPWT
SAHGTSTGVPWP
VPWMEPAYQRFL
TLPWLEESYWRP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17187899</Reference>
<Target_Name>Umbilical endothelial 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.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The biopanning is performed in parallel on three different groups of endothelial cells: (a) cells incubated under normal oxygen conditions; (b) after 3h of hypoxia; (c) after 24h of hypoxia.
Peptides obtained did not induce VEGF receptor gene expression,indicating the template is not VEGF.</Brief_Description>
<BiopanningDataSet_Comments>The authors have isolated 40 individual phage clones from each group of endothelial cell screenings. A total of 15 non-identical sequences were obtained. However, only 6 unique sequences were given in the published paper. QPWLEQAYYSTF, YPHIDSLGHWRR and LLADTTHHRPWT originated respectively from endothelial cells under normoxia, 3 and 24h of hypoxia. SAHGTSTGVPWP was identified on cells under 3 and 24h of hypoxia. VPWMEPAYQRFL was found in both normoxia and 24h hypoxia cell groups. TLPWLEESYWRP is common to endothelial cells under normoxic and hypoxic conditions. These peptides induced angiogenesis as demonstrated by endothelial cell proliferation, migration and tube formation. Injection of peptides into the ears of mice resulted in increased numbers of blood vessels. They did not induce VEGF receptor gene expression indicating a possible VEGF unrelated mechanism.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>361</BiopanningDataSetID>
<Peptides>VLIMPVLLGIPLLC(0.7)
VXNCERITISRILN(0.1)
VXNCERITISQNSKL(0.1)
RSLNHASSFGYSVIM(0.1)</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:17959143</Reference>
<Target_Name>Proteinase K</Target_Name>
<Template_Name>Protease inhibitors</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>pComb3 X15 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>VLIMPVLLGIPLL inhibits proteinase-K activity with an inhibition constant of 4 μM. VLIMPVLLGIPLL revealed a considerable homology with a short peptide stretch of the Kuniz-type serine-protease inhibitor from Caenorhabditis elegans.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>362</BiopanningDataSetID>
<Peptides>VWNCERITISRLIN(0.5)</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:17959143</Reference>
<Target_Name>Cathepsin S</Target_Name>
<Template_Name>Protease inhibitors</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>pComb3 X15 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>VWNCERITISRLIN showed functional inhibition of cathepsin-S induced sprouting of endothelial cells.Its IC50 is 13 μM. VWNCERITISRLIN showed homology with serine-protease inhibitor 8 from Rattus norvegicus.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>363</BiopanningDataSetID>
<Peptides>CLRNSPRKQADRILNC(0.6)</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:17959143</Reference>
<Target_Name>Cathepsin S</Target_Name>
<Template_Name>Protease inhibitors</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>pComb8 CX15C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The IC50 0f this peptide for cathepsin-S inhibition is 26 μM.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>364</BiopanningDataSetID>
<Peptides>THALWHT(4)
FDFWITP(3)
SHALWHT(1)
VPAVPLD(1)</Peptides>
<Motif>THALWHT</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:18040053</Reference>
<Target_Name>Hronchial epithelial cells (16HBE14o-)</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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>365</BiopanningDataSetID>
<Peptides>FDFWITP(7)
FDFWLTP(1)
FYALEFP(1)</Peptides>
<Motif>FDFWITP</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18040053</Reference>
<Target_Name>EGTA-treated 16HBE14o- cell monolayers</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>Before they were used to screen the library, monolayers of human bronchial epithelial cells (16HBE14o-) were treated with a calcium chelator, EGTA, to increase accessibility to the junctional complex/paracellular space.</Brief_Description>
<BiopanningDataSet_Comments>FDFWITP might be binding to the tight junction complex or other cellular components that are more available as a result of EGTA treatment.FDFWITP, identified as a potential tight junction modulator.
</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>366</BiopanningDataSetID>
<Peptides>MMFKGQRVERVLT
HNEFRQRETYMVF
NWQEFQAKRSVAY
LELKSNSVIMRWP
DYNEVRRQMSMQM
ALEMRAADVEYHF
VEHLMEVQRKTTW
GVEVKRQLSYHYM
QELVGANIETYML
QQMEVSRYVQYKW
LQSFRQAPVDIWW
QELRGKISIQPFK
QQEYMSGQYDIIF
SMEFAATVTSTFE
EQQLKGRQTHIII
MELKGQTDMFYII
GAYAVGRWSYVDA
GQFATSPKITIHK
DVQEFRGVTAVIR
HEARTVSTTYLML
YMEMRGSTTVFFN
QELIGSYSVMPTN
HYYMEATRDIEMV
NEAHSSGITIMLR
DHPMEFRSKITMK
TFAEMKGTVSYAL
GVHMESMRRYTVI
FQEYTGTYDIMDP
FQAVEASKTLHFW
YLETSRTYTTVWP
TDYLEVRSQPIIY
TFEQEVRAPNISW
PQEVQGIAVEWV
AEAKASTLHVYLM
DYMEVVGNKISYI
VIMEAVGRKTILQ
FQAEAARAVTYSS
EDYVYVKDVGTTN
QEYKAHHSYKLMS
YNEYRATPTFAVV
EYFHANTTRIVQS
ALEASRFISWDIN
WEAVAAPIMHTWV
FQELKAAETFWM
NTLYAVAPPVIYV
FQPYEVQRITTVM
KPMESGRRTTVYY
MEFKGALQYRLQP
PQEVKQARKWIIE
YRQQEVKRHIQIV</Peptides>
<Motif>E-[AFVLMI]-x(0,1)-[RK]-x(2,3)-[ST]-[VYIFWMLA]</Motif>
<Unique_Sequence_Number>50</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:17311924</Reference>
<Target_Name>A disintegrin and metalloproteinase with thrombospondin motifs 4</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>X13 phage libray</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>ADAMTS-4 was cloned and expressed in Drosophila Sf9 cells. The purified preparation was composed almost solely of the 70-kDa active form.</Brief_Description>
<BiopanningDataSet_Comments>The authors have identified the ADAMTS-4 cleavage motif E-[AFVLMI]-X(0,1)-[RK]-X(2,3)-[ST]-[VYIFWMLA], with Glu representing P1. Several 13-mer peptides such as DVQEFRGVTAVIR and HNEFRQRETYMVF, were shown to be substrates for ADAMTS-4.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>367</BiopanningDataSetID>
<Peptides>CRKRLDRNC(8)
CMNPKKQRC(4)
CRSTKSSAC(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:19012727</Reference>
<Target_Name>Human primary atherosclerotic tissues</Target_Name>
<Template_Name>Interleukin-4, IL-4</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Primary human atherosclerotic tissues were obtained by endarterectomy of three patients with coronary atheroma (50 ± 12 year-old). Cell suspensions were prepared by homogenizing the tissues.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-seven phage clones from coronary atheroma tissues were randomly picked and sequenced. However, only 3 unique sequences were given in the published paper. It has been demonstrated that the CRKRLDRNC peptide homes to atherosclerotic plaques through binding to IL-4R. CRKRLDRNC is a mimic of IL-4(P05112). According to the BLAST results, CMNPKKQRC may be a mimic of integrin β2 precursor(P05107); and CRSTKSSAC, Thrombospondin-4 precursor(P35443).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>368</BiopanningDataSetID>
<Peptides>CPSNGKRDC(2)
CFSEVD(2)
CRQGGKRDC(1)
CRTTRSKTC(1)
CRTTQSNTC(1)
CMHSEVD(1)
CLIGEVD(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:19012727</Reference>
<Target_Name>Human primary atherosclerotic tissues</Target_Name>
<Template_Name>Interleukin-4, IL-4</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Primary human atherosclerotic tissues were obtained by endarterectomy of three patients with femoral atheroma (63 ± 11year-old). Cell suspensions were prepared by homogenizing the tissues. </Brief_Description>
<BiopanningDataSet_Comments>Twenty-seven phage clones from femoral atheroma tissues were randomly picked and sequenced. However, only 7 unique sequences were given in the published paper. The BLAST results indicate that the templates of the obtained peptides might include MMP-16(P51512), Scavenger receptor class A member 3(P35443) and Toll-like receptor 4 precursor(O00206).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>369</BiopanningDataSetID>
<Peptides>THFATMF
LQPTMHK
FKPPASL
AEFAFNF
NAPSRNQ
NPRPLSI
SHYVNSQ
EGLHQRK
HPQHAGG
HTSHLSC
WPSFPIP
TPALQFP
SFTWAPD
APPYTAY
SWPSHVP
HPNLLSP
NEYPPNP
NPNWGPR
TRRETPA
HTTHHRN
VETWRPN
ERFIDTQ
TTHQFPF</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>23</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17907769</Reference>
<Target_Name>Melanin</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>Melanin was purified from MNT-1 human melanoma cells.</Brief_Description>
<BiopanningDataSet_Comments>The final eluate yielded approximately 50 individual clones; 24 clones from the plate were chosen at random and sequenced. Not 24, but 23 unique sequences were given in the published paper. Among them, 8 best tumor melanin-binding phages were identified by ELISA. Of the 8 phages, 3 best binding phages were identified as HTTHHRN, NPNWGPR and TTHQFPF.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>370</BiopanningDataSetID>
<Peptides>HPMHFPS(11)
YPRWQIP(6)
SVFWMIP(6)
YPQLPFT(4)
HPMHFPC(1)
HHYAFSV(1)
SPNVNAN(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17711505</Reference>
<Target_Name>HBJ127</Target_Name>
<Template_Name>Natural killer cells antigen CD94</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>Thirty clone were randomly picked and sequenced after the third round of panning. Seven unique sequences were obtained.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>371</BiopanningDataSetID>
<Peptides>PSRALL(1)
GRRALC(1)
HRALSR(1)
HRALRG(1)</Peptides>
<Motif>RAL</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:17252013</Reference>
<Target_Name>Kasumi-1 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>X6 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>After the third and fouth rounds of selection, 11 and 12 clones were randomly picked and sequenced respectively. PSRALL and GRRALC were from the 3rd round; HRALSR and HRALRG, the 4th round.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>372</BiopanningDataSetID>
<Peptides>CPLDIDFYC(7)
CRGLGRALC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:17252013</Reference>
<Target_Name>Kasumi-1 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>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The template of CPLDIDFYC might be Vascular Cell Adhesion Molecule 1 (VCAM-1), since the α4β1 integrin (VLA-4) has been identified as the target of CPLDIDFYC.</Brief_Description>
<BiopanningDataSet_Comments>After the third and fouth rounds of selection, 11 and 19 clones were randomly picked and sequenced respectively. CRGLGRALC was from the 3rd round; CPLDIDFYC, the 4th round.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>373</BiopanningDataSetID>
<Peptides>AWYPLPP(37)
VQKHVHP(2)
LGVCPPS(1)
HAIYPRH(1)
TQAKPKL(1)
AATNLGI(1)
QLHRHHH(1)
APNLRPQ(1)
KPVQLDH(1)
KMLQSSV(1)
WSYHRLP(1)</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:16806673</Reference>
<Target_Name>Hepatocellular carcinoma cell line HCCLM3</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>HCCLM3 has a high metastatic potential. The phage-displayed random peptide library was first screened with MHCC97L which is an HCC cell line with a low metastatic potential. The unbound phages remaining in supernatant were then screened HCCLM3.</Brief_Description>
<BiopanningDataSet_Comments>AWYPLPP was identified as a specific peptide ligand that binds to the cell surface of highly metastatic human hepatocellular carcinoma (HCC). This peptide was able to promote in vitro invasion of highly metastatic HCC cells by activating matrix metalloproteinase-9 and in vivo lung metastasis of HCC tumors.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>374</BiopanningDataSetID>
<Peptides>GSSSWWQRWWPPW(14)
GPMESLQAFWPPW(1)
GVFLLKQVPQPSH(1)
GRLWWLQLFEPGH(1)
GLRKVPQSVPPDM(1)
GHFLKPQVLRPTR(1)
GQFMMRQYWPPVH(1)
GLLKYQQWASPLC(1)
GYFWYDQPWQPEQ(1)
GRNHYIQRDNPVS(1)
GVFHVLQNAIPQY(1)
GTMPNMQHHDPAR(1)
GTRYLVQYLFPHL(1)
GRPATQQGLTPAR(1)
GYIGTYQQWNPPP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17268054</Reference>
<Target_Name>Human epidermoid carcinoma A431 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>Tat-based pCANTAB-5E library library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Cells on culture plates were incubated with the peptide-phage library for 2h at 37°C with shaking every 15min during the round of panning. Following this, the cells were washed 20 times with PBS at room temperature. After washing, the cells were lysed. 100ml lysate was used to infect E. coli and then used in the next round of selection.</Brief_Description>
<BiopanningDataSet_Comments>The GSSSWWQRWWPPW peptide did not exhibit cytotoxicity when recombined with PSIF. This result indicated that this tryptophan-rich peptide binds to the cell membrane but does not penetrate through to the cytoplasm.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>375</BiopanningDataSetID>
<Peptides>IQSPHFF(19)
HHSHRHH(4)
HHHHLSM(2)
VHPPLLT(1)
KNVHVPL(1)
GGHSTPE(1)
DVTTPSP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17653285</Reference>
<Target_Name>Genhance 680, GH680</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>GH680 was covalently coupled to BSA and then immobilized on Nunc Maxisorp plates for selection. A subtraction well containing a BSA-only sample was prepared. The subtraction step was designed to filter BSA-and/or plastic-binding clones.</Brief_Description>
<BiopanningDataSet_Comments>IQSPHFF has nanomolar affinity for near infrare fluorochromes. The developed peptide sequence allows detection of NIR dyes in a wide range of assays including ELISA, flow cytometry, high throughput screens, microscopy, and optical in vivo imaging.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>