<result><BiopanningDataSet><Item><BiopanningDataSetID>1176</BiopanningDataSetID>
<Peptides>LPYSHKFMIHSKPTF(6)
PQHYKMPVRPYSIHS(4)
SSTRSLTFDFNMLHS(4)
MDAQHLVALHDVAFY(4)
SCCTHSTPALPQLPS(4)
NAVAHQAVGPAPFLS(3)
WTPSTLSHYMTSPFY(2)
HLLTHKAHDNAYYAK(2)
PTPCHGQVDELHAAV(1)</Peptides>
<Motif>[IL]-H-S</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11245205</Reference>
<Target_Name>Cellulose-binding domain (CBD)</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>X15 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The sequence I/LHS, which was found to be an efficient binder of CBD, was fused to a synthetic gene of HRP as an affinity tag. The tagged enzyme (tHRP) was then immobilized on microcrystalline cellulose coated with CBD, thereby demonstrating the indirect immobilization of a protein to cellulose via three amino acids selected by phage display library and CBD.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1177</BiopanningDataSetID>
<Peptides>KLWVIPQ(3)
KLWVLPK(2)
KLWQVFP(1)
KVWILTP(1)
KVWTIPR(1)
KVWYITP(1)
KCCYIPT(4)
KGPPITR(1)
KVWDLRS(1)
YVTREPR(1)</Peptides>
<Motif>K-B-W-x-B-[PTRF]-x</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:12549820</Reference>
<Target_Name>DNA topoisomerase 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>Before applying phage display library to htop(1-214) prepanning step was performed with albumin (100µg/ml) as a target.</Brief_Description>
<BiopanningDataSet_Comments>The consensus sequence identified for clones binding to the N-terminal domain was found in 35 human proteins that are either permanently or temporarily located in the nucleus. They are in majority involved in the DNA repair, transcription, RNA metabolism or cell cycle control. Four of identified proteins: Bub3 protein, Cockayne syndrome protein A, damaged DNA binding protein 2 and GRWD protein belong toWD-repeat proteins and their sequences recognized by the N-terminal domain are identically localized.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1178</BiopanningDataSetID>
<Peptides>LPPSIPR(11)
NLRPSIP(9)
LLPSIPF(7)
LIPSITW(3)</Peptides>
<Motif>L-x-P-S-I-P</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12474050</Reference>
<Target_Name>Anti-JL1 leukemia-specific monoclonal antibody</Target_Name>
<Template_Name>JL1 antigen</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 phage library was pre-incubated with an irrelevant mAb (IgG1, kappa) for 30 min and then added into the well coated with anti-JL1 mAb.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1179</BiopanningDataSetID>
<Peptides>LPPSIPFGLTVG(16)[5.63]
LLPSIPNQAYLG(14)[6.50]</Peptides>
<Motif>L-x-P-S-I-P</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:12474050</Reference>
<Target_Name>Anti-JL1 leukemia-specific monoclonal antibody</Target_Name>
<Template_Name>JL1 antigen</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>Surface plasmon resonance (SPR)</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The interaction between anti-JL1 mAb and the mimetic peptides was tested using a surface plasmon resonance biosensor. The Kd (μM) value was measured and shown. </Affinity_Measurement_Description>
<Brief_Description>The phage library was pre-incubated with an irrelevant mAb (IgG1, kappa) for 30 min and then added into the well coated with anti-JL1 mAb.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1180</BiopanningDataSetID>
<Peptides>CHQKPWEC(17)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 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>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1181</BiopanningDataSetID>
<Peptides>CHQKPWEC(14)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 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>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1182</BiopanningDataSetID>
<Peptides>CKDRFERC(17)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 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>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1183</BiopanningDataSetID>
<Peptides>CKDRFERC(14)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 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>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1184</BiopanningDataSetID>
<Peptides>CNWTDKTC(4)
CNITQKSC(4)
CNVSDKSC(2)</Peptides>
<Motif>N-x-[ST]-D-K-[ST]</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:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 3</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1185</BiopanningDataSetID>
<Peptides>CNVSDKSC(13)
CNKTDKGC(2)
CNWTDKTC(1)</Peptides>
<Motif>N-x-[ST]-D-K-[ST]</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12496764</Reference>
<Target_Name>Purified IgGs from serum of prostate cancer patient 3</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX6C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>First, a pre-clearing step was used to remove nonspecific clones by pre-absorbing the phage peptide library onto purified IgGs from normal serum pooled from volunteer agematched blood-donor control men. Next, the pre-cleared phage library was selected onto the pool of IgGs purified from the serum of prostate cancer patients.</Brief_Description>
<BiopanningDataSet_Comments>Authors identified a consensus motif, NX[ST]DK[ST], that bound selectively to circulating antibodies from cancer patients over control antibodies from blood donors. Authors validated this motif by showing that positive serum reactivity to the peptide was specifically linked to disease progression and to shorter survival in a large patient population.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1186</BiopanningDataSetID>
<Peptides>STVPRMPLSPPN
FMNPLHPRVLRP
NYVIHDVPRHPA
VNMGNYRQQQPL
SMLDLFPRAASY
SVYNVRPSSLSA
TVMASPTMKSNS
VNMGNYRQQQPQ
KFPGPNCCHALP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:12409405</Reference>
<Target_Name>Mycobacterium paratuberculosis</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1187</BiopanningDataSetID>
<Peptides>SLRLLQWFLWAC(6)</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:11318108</Reference>
<Target_Name>Deoxyribonuclease-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 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>One conserved sequence (SLRLLQWFLWAC) was found in six colonies, while all other sequences appeared only once.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1188</BiopanningDataSetID>
<Peptides>RLQAWWEMWADSYRP(5)[0.80 ± 0.03]
QKRPVNISTLQELWE(3)[0.34 ± 0.02]
SVQARWEAAFDLDLY(3)[0.52 ± 0.09]</Peptides>
<Motif>[LV]-Q-[AE]-x-W-E</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:12542398</Reference>
<Target_Name>Anti-human IFN-b monoclonal antibody YSB-2</Target_Name>
<Template_Name>Interferon beta, IFN-beta</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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbances at 450 nm was measured. Data, means ± S.D. from triplicate wells, were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Authors screened a random phage display library with a soluble form of the human type I IFN receptor (sIFNR) and a neutralizing monoclonal antibody (mAb) against IFN-b. Three clones were identified as binding YSB-2 ,but screening with sIFNR failed to identify any peptide ligands.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1189</BiopanningDataSetID>
<Peptides>YAPYGL(2)[88/82]
WLPSSI(1)[96]
RLPLGI(1)[94]
QRPHAI(1)[93]
KGPIHL(1)[91]
FLPQGW(1)[90]
LDPWSY(1)[81]
LLGLRN(1)[91]
QLLGFL(1)[90]
AVVQHL(1)[89]
NALASI(1)[88]
ARLGHF(1)[85]
GAVKHL(1)[81]
GAARHI(1)[79]
NLRSKL(1)[79]
NLKSRV(1)[77]
DRQMAL(1)[69]
FSMFSL(1)[66]
WAKSNL(1)[48]
VSLKNL(1)[45]
TVGWIS(1)[33]
VASGIY(1)[86]
PQHVRQ(1)[71]
AVYFHM(1)[66]
LRAMQT(1)[65]
GANSLK(1)[63]
RIGFLR(1)[88]
VFSIPL(1)[79]
RAMHMY(1)[79]
RSENIR(1)[79]
IKYHSL(1)[77]
LISHSI(1)[73]
ARYRWL(1)[72]
GVSMPF(1)[67]
VMSIRI(1)[61]
RSYAIL(1)[55]
SRRLHL(1)[50]
FIANPV(1)[42]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>38</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11959855</Reference>
<Target_Name>Matrix metalloproteinase-14, MMP-14</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X6 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Individual phage were analyzed after three rounds of selection by MT1-MMP. The substrates are grouped according to their ability to be hydrolyzed by MT1-MMP, relative to non-treated controls, as
measured by substrate phage ELISA and expressed as % hydrolysis.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Two-hundred clones were screened for their ability to be hydrolyzed by MT1-MMP using the substrate phage ELISA we reported previously. Forty of the two-hundred clones were cleaved efficiently by MT1-MMP and were carried forward for additional analysis.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1190</BiopanningDataSetID>
<Peptides>CPEFVDVEGDPGALLAC
CGWVDVIASGDTATLAC
CDVEWVDVSSLEWDLPC
CLMGCWCDVGVGGESLC
CPDWVDVFKLVEGVMLC</Peptides>
<Motif>[ED]-[WF]-[VC]-D-V</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5-7</Rounds_of_Panning>
<Reference>PMID:12393589</Reference>
<Target_Name>P-selectin</Target_Name>
<Template_Name>P-selectin glycoprotein ligand 1</Template_Name>
<Structure_of_Target_Template_Complex>1G1S,</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>In fact, chimeric P-selectin, consisting of human IgG1 fused to the binding domain of human P-selectin (PS-IgG), was the target.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1191</BiopanningDataSetID>
<Peptides>VGLDPRDWVDVSDYA
DWVDVREVLTGEQRV</Peptides>
<Motif>DWVDV</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:12393589</Reference>
<Target_Name>P-selectin</Target_Name>
<Template_Name>P-selectin glycoprotein ligand 1</Template_Name>
<Structure_of_Target_Template_Complex>1G1S,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>pIF4 X15 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In fact, chimeric P-selectin, consisting of human IgG1 fused to the binding domain of human P-selectin (PS-IgG), was the target.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1192</BiopanningDataSetID>
<Peptides>ECSEGWCDMKIDRLDAGG
WCDSVGDRAGPSV</Peptides>
<Motif>WCD</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:12393589</Reference>
<Target_Name>P-selectin</Target_Name>
<Template_Name>P-selectin glycoprotein ligand 1</Template_Name>
<Structure_of_Target_Template_Complex>1G1S,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>pIF4 X28 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In fact, chimeric P-selectin, consisting of human IgG1 fused to the binding domain of human P-selectin (PS-IgG), was the target.</Brief_Description>
<BiopanningDataSet_Comments>The isolated peptide sequences were not displayed completely.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1193</BiopanningDataSetID>
<Peptides>FLHTRLFVSDWYHTP(2)
SRAPRFPWLNPLDGW(2)
TFTRVVTDVYRPRLS(2)
EDFRFESSLSINDHA(2)
GWHTRIFVSDWYHTP(1)
SLAPRFPWLNPLDGW(1)
SRSPRFPWLNPLDGW(1)
TFMRVVTDVYRPRLS(1)
SFTRVVTDVYRPRLS(1)
DFRFESSLSINDHA(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:12472892</Reference>
<Target_Name>Anti-L2/HNK-1 monoclonal antibody L2-412</Target_Name>
<Template_Name>L2/HNK-1 carbohydrate</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>For the second and third rounds of screening, the phages were preincubated with rat IgG (100 μg/mL) to decrease non-specific binding. </Brief_Description>
<BiopanningDataSet_Comments>The phages isolated from a 15-mer peptide library by adsorption to this antibody share a consensus sequence of amino acids. The peptide mimicked several important functions of the L2/HNK-1 carbohydrate, such as binding to motor neurons in vitro, and preferential promotion of in vitro neurite outgrowth from motor axons compared with sensory neurons.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1194</BiopanningDataSetID>
<Peptides>VTWRMWYVPA(2)
VVHMRYSFRI(5)
YEIRFRYLQF(4)
TGYRLVIYRL(1)
ASTIRISFFV(3)
AIRIVIATNI(3)
SEGAVVFHAT(2)
KIQLQWIVSL(2)
YSGSLVLIVR(2)
SHSLKLTLVI(4)
MMKVVFRWSD(1)
TLGGGLLLWH(1)
VPVLHWTVMF(1)
RVVYISAMVT(1)
LVVINITYDR(1)
AWTSPVDSFQ(1)
YLHIVFQVPT(1)
PRGYWLRIEW(1)</Peptides>
<Motif>RMRY</Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9531425</Reference>
<Target_Name>Cholesteryl ester transfer protein</Target_Name>
<Template_Name>Cholesteryl esters, CE</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>X10 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Of the 36 randomly chosen clones, phage displaying VTWRMWYVPA, VVHMRYSFRI, YEIRFRYLQF and TGYRLVIYRL exhibited relatively high binding to CETP (OD450 0.4-0.7), whereas the remaining 24 clones displayed only moderate to low binding to CETP in the reported assay system. The synthesized VTWRMWYVPA inhibited CETP-catalyzed transfer of cholesteryl esters and triglycerides. Amino- and ciirboxy-terminal truncations demonstrated that the original decapeptide could be reduced to a pentapeptide without loss of either its ability to bind to CETP or its ability to inhibit CETP-mediated lipid transfer. That pentapeptide, WRMWY bound directly to CETP and its inhibition was consistent with that of a competitive inhibitor of CETP.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1195</BiopanningDataSetID>
<Peptides>SRPKPPNPS(15)[NT]
KRGSIIPNG(5)[1.225, 1.267, 2.066]
KTKKPPNPS(4)[NT]
RLKPPNPTE(2)[NT]
KPKTNQIRP(2)[NT]
YTTTLSFQK(2)[NT]
GVHRLTRPS(1)[1.035, 5.124, 0.888]
GLHRSQTSM(1)[0.904, 4.587, 1.031]
GRHHWASGP(1)[0.933, 5.390, 1.314]
GQHKSRSFP(1)[0.976, 7.768, 0.664]
RKPPNPPPP(1)[NT]
KPPNPTRPE(1)[NT]
KPPNPRPSL(1)[NT]
RPSKPPNPV(1)[NT]
KALKPPNPV(1)[NT]
RRDTISPYS(1)[NT]
KKTGNITPK(1)[NT]
GQHHSLSTP(1)[NT]
GAHASLWTP(1)[NT]
GSHLSARAP(1)[NT]
GMHKSVFAT(1)[NT]
DTTLNYRGA(1)[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>22</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:9532590</Reference>
<Target_Name>IgG from the cerebrospinal fluid (CSF) of multiple sclerosis (MS) patients</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>pVIII-9aa phage display library (X9)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of the selected phagotopes to the CSF1, CSF2 and CSF3 was detected by ELISA on immobilized phage, respectively. For each sample antibody recognition of the tested phagotope and wild type phage was measured. Average values (A405nm) from two independent experiments have been determined. Results are expressed as the ratio between the average value of the tested phagotope and that of wild type phage (clone/wt A405 nm). Data shown were reproduced from the graph. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>For each selection, 5 microgram of CSF IgG were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab. Eluted phages were subjected to immunological screening using the same CSF as probes.</Brief_Description>
<BiopanningDataSet_Comments>Positive plaques were individually picked and rescreened using CSF from MS patients and from patients affected by other neurological diseases. Fifty-seven phages positive only to the MS CSF were identified. Their sequences were mixed together in the original paper, though the two libraries were selected separately.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1196</BiopanningDataSetID>
<Peptides>WLQDITL(1)
IDQDITV(1)
QQDITVH(1)
QDITLRP(1)
HIRRILL(2)
YPMIISP(1)
ENGADVD(1)
VHPPPFL(1)</Peptides>
<Motif>QDIT</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9598980</Reference>
<Target_Name>Anti-syndecan-1 monoclonal antibody B-B2</Target_Name>
<Template_Name>Syndecan-1, SYND1</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>B-B2 was produced by ascitic fluid and purified on a protein A column. Coated mAb was used to select the phages which were then eluted with an acidic treatment, and amplified in bacteria for the next round of selection. After the third round of selection bound phages were eluted by adding the selecting mAb as competitor.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1197</BiopanningDataSetID>
<Peptides>IQDITLS(1)
RQDITLV(1)
GHTQDIT(1)
QDITLFN(4)
QDITMFV(2)
MQNITLF(1)
QNITLSQ(1)</Peptides>
<Motif>QDIT</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:9598980</Reference>
<Target_Name>Anti-syndecan-1 monoclonal antibody B-B2</Target_Name>
<Template_Name>Syndecan-1, SYND1</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>B-B2 was produced by ascitic fluid and purified on a protein A column. Coated mAb was used to select the phages which were then eluted with an acidic treatment, and amplified in bacteria for the next round of selection. After the third round of selection bound phages were eluted by adding the selecting mAb as competitor and then acidic conditions were applied to recover the remaining phages.</Brief_Description>
<BiopanningDataSet_Comments>Independently of the elution procedure used, the number of recovered phages was at least 30 times higher from the well coated with the selecting mAb than with an irrelevant control mAb, suggestting that the selected phages were mAb specific.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1198</BiopanningDataSetID>
<Peptides>LTLPEVA(1)
APLPEVL(1)
HLPEVSP(1)
FLPEVLL(1)
YLPEVIS(1)
YLPEVLP(1)
YLPEVQP(2)
FLPDVAS(1)
FLPDVLS(1)
YLPQVAS(1)
LTDVRTP(1)
TTNDFTR(1)</Peptides>
<Motif>LPEV</Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9598980</Reference>
<Target_Name>Anti-syndecan-1 monoclonal antibody B-B4</Target_Name>
<Template_Name>Syndecan-1, SYND1</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>B-B4 was produced by ascitic fluid and purified on a protein A column. Coated mAb was used to select the phages which were then eluted with an acidic treatment, and amplified in bacteria for the next round of selection. After the third round of selection bound phages were eluted by adding the selecting mAb as competitor.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1199</BiopanningDataSetID>
<Peptides>ILPEVVS(1)
TLPEVLS(1)
QLPEVSS(1)
ALPEVLS(1)
MLPEVLP(1)
LELPEVM(1)
VLQEVSS(1)
AFPSPTL(1)
AYTSAHK(1)</Peptides>
<Motif>LPEV</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9598980</Reference>
<Target_Name>Anti-syndecan-1 monoclonal antibody B-B4</Target_Name>
<Template_Name>Syndecan-1, SYND1</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>B-B4 was produced by ascitic fluid and purified on a protein A column. Coated mAb was used to select the phages which were then eluted with an acidic treatment, and amplified in bacteria for the next round of selection. After the third round of selection bound phages were eluted by adding the selecting mAb as competitor and then acidic conditions were applied to recover the remaining phages.</Brief_Description>
<BiopanningDataSet_Comments>Independently of the elution procedure used, the number of recovered phages was at least 30 times higher from the well coated with the selecting mAb than with an irrelevant control mAb, suggestting that the selected phages were mAb specific.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1200</BiopanningDataSetID>
<Peptides>WWIWWPGSVE(4)
WWGPVIMWDA(2)
WFSWGFPQWW(1)
VWWSLLVPLA(4)
SWGFPVFWHR(1)
STGFPIFWHS(1)
PEGEYAWWVE(1)
DWWSYAWTLV(1)
WLWVSRWPGG(2)
WWLLWTIPSW(1)
GMWWWPLFTL(1)
PQVWGVWTDE(1)
VLNWPGMLLV(1)
WHLACAGVFS(1)
WWTLIYLMP(1)</Peptides>
<Motif></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:9661811</Reference>
<Target_Name>MDDQRDLISNNEQLK peptide</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 X10 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>When screening a large number of individual phage clones for binding to biotinylated Ii peptide (MDDQRDLISNNEQLK) coupled to microtiter wells, seven phage clones binding significantly above background level were identified. Sequencing of phage inserts revealed that one displayed WFSWGFPQWW, two had insert WWGPVIMWDA, and four contained WWIWWPGSVE.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>