<result><BiopanningDataSet><Item><BiopanningDataSetID>1626</BiopanningDataSetID>
<Peptides>APLLTWPRAIGP(0.166)
MNNSLLPMRLQT(0.166)
VPVQTQRNFLSI(0.166)
DIHSPTRQSPYY(0.166)
SPSHQWPSPKGS(0.166)
SSSQTDNRMSAG(0.166)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19539948</Reference>
<Target_Name>Semiconductor InP(001) surface</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>1627</BiopanningDataSetID>
<Peptides>HAPGNMLRVSLG(0.5)
YAIKGPSHFRPS(0.5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19539948</Reference>
<Target_Name>Semiconductor InP(001) surface</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>1628</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(1.0)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:19539948</Reference>
<Target_Name>Semiconductor InP(001) surface</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>1629</BiopanningDataSetID>
<Peptides>AANDKMQKFRLV(0.111)
GFDKIPLDMMRG(0.111)
ITPHHATLPQSR(0.111)
DYQFKSSPLRET(0.111)
KWPGNSMFPYGF(0.111)
QYPYLLSAGDIH(0.111)
QSTPTRPGMLLL(0.111)
TNKPSFTPLTAS(0.111)
YTITPNPLPSNP(0.111)</Peptides>
<Motif></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:19539948</Reference>
<Target_Name>Semiconductor InP(111) surface</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>1630</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(0.8)
SSPLHQQSHYTY(0.2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19539948</Reference>
<Target_Name>Semiconductor InP(111) surface</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>1631</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(1.0)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:19539948</Reference>
<Target_Name>Semiconductor InP(111) surface</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>1632</BiopanningDataSetID>
<Peptides>CIFPLCLGRPIAASYPPKTR(1)[0.908 ± 0.041, 0.598 ± 0.008]
LNSRHTDKGTVQFALIAVRG(1)[1.064 ± 0.065, 0.957 ± 0.010]
YVALQGSMFDRVRVFWMARG(1)[0.826 ± 0.033, 0.442 ± 0.017]
ACSDRFLRRPMCLPPHVVFL(1)[1.146 ± 0.008, 0.303 ± 0.025]
GFGKDITTGHSFTHKSNNDP(1)[0.836 ± 0.029, 0.373 ± 0.024]
TTGNLSLDLLIATRFSSHGK(1)[0.948 ± 0.021, 0.880]
IHTDRPAWKYVGALPVIHVR(1)[0.220 ± 0.006, 0.223 ± 0.024]
NSNFTVHSNYWYWNRYIPPV(1)[1.046 ± 0.019, 0.945 ± 0.009]
TNLLYMLNTEAQYKALFMRK(1)[0.871 ± 0.024, 0.492]
ILPNPIHHTWLPFKLSHNLP(1)[0.609 ± 0.019, 0.557 ± 0.062]
GCSYPMCRFNVVRFTGLSLL(1)[1.166 ± 0.009, 0.680 ± 0.021]
GLFDLTNYYYLSRGTQIKGT(1)[0.707, 0.663 ± 0.022]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19095030</Reference>
<Target_Name>Anti-EG95 polyclonal antibody</Target_Name>
<Template_Name>EG95</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>X20 fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage binding to anti-EG95 polyclonal antibody was measured in the absence or presence of the protein competitor (EG95-MBP) by ELISA. The absorbance at 450 nm was determined. Displayed values are reproduced from the graph and expressed as the mean ± SEM of duplicate wells. The absorbance of the phage R1 as negative control was 0.110 both in the absence or presence of the protein competitor (EG95-MBP).</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1633</BiopanningDataSetID>
<Peptides>NRLFDRVDRFYA(1)[1.292 ± 0.065, 0.975 ± 0.057]
GKPGWLLDNVAL(1)[0.851 ± 0.022, 0.108 ± 0.014]
HYKWLNDPLAAR(1)[0.916 ± 0.036, 0.426 ± 0.007]
TLFGRMEHYFN(1)[1.277 ± 0.054, 1.123 ± 0.023]
ISTSKPAWKLAN(1)[1.268 ± 0.050, 0.186 ± 0.032]
CIPPLCKLRLHE(1)[1.168 ± 0.100, 0.541 ± 0.087]
LDKRNNDPFHLP(1)[0.904 ± 0.168, 0.123 ± 0.018]
SVSVGMKPSPRP(1)[0.474 ± 0.014, 0.371 ± 0.015]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19095030</Reference>
<Target_Name>Anti-EG95 polyclonal antibody</Target_Name>
<Template_Name>EG95</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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage binding to anti-EG95 polyclonal antibody was measured in the absence or presence of the protein competitor (EG95-MBP) by ELISA. The absorbance at 450 nm was determined. Displayed values are reproduced from the graph and expressed as the mean ± SEM of duplicate wells. The absorbance of the phage R1 as negative control was 0.110 both in the absence or presence of the protein competitor (EG95-MBP).</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1634</BiopanningDataSetID>
<Peptides>VSQTMRQTAVPLLWFWTGSL
YAAWPASGAWTGTAPCSAGT</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:16386888</Reference>
<Target_Name>H1299 cell line</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>IR20 phage display library (X20)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>A cell-targeting Peptide YAAWPASGAWTGTAPCSAGT, which represented 10 of the 12 clones sequenced, was isolated at round 5. The isolated phage clone binds H1299 cells 80 times better than a control phage and can distinguish between H1299 and normal control cells. The phage clone also binds to the lung pleura epidermoid cell line, Calu-1 but not to all lung carcinoma cell lines. The peptide is functional outside the context of the phage and tetramerization of the peptide on a trilysine core improves the affinity of the peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1635</BiopanningDataSetID>
<Peptides>SHRLHAT*ILMP(1)[1.680]
SHRILSSALV*V(1)[1.530]
SHRLHNTMPSES(1)[2.006]
THRLYLASTLPG(1)[1.685]
SHRLPHPNLIRL(1)[1.830]
QHRIHNPAPVSL(1)[2.083]
HHRILIEPPSMH(1)[1.685]
SHRLPPVSNPSL(1)[1.607]
HHRLNNQDDLLK(1)[1.860]
SHKLFYQMGTQL(1)[1.573]
QHRMTWMQGLSS(1)[1.685]
QHKLYPVIPLPS(1)[2.100]</Peptides>
<Motif>H-[RK]-[LI]</Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:13679612</Reference>
<Target_Name>Anti-DENV2 monoclonal antibody Ab4</Target_Name>
<Template_Name>Dengue virus 2, DENV2</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X12 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, the absorbance at 490 nm was measured. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Selected phage clones reacted specifically with Ab4 and did not react with other mAbs. Immunopositive phage clones displayed a consensus motif, His-Arg/Lys-Leu/Ile, and a synthetic peptide corresponding to the phage-displayed peptide bound specifically to Ab4. The His and Arg residues in this epitope were found to be crucial for peptide binding to Ab4 and binding activity decreased dramatically when these residues were changed to Leu. The epitope-based synthetic peptide not only identified serum samples from DEN-2-immunized mice and rabbits by ELISA but also differentiated clearly between serum samples from DEN-2- and Japanese encephalitis virus-immunized mice.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1636</BiopanningDataSetID>
<Peptides>SMSIARL
VSFLEYR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:11830668</Reference>
<Target_Name>Mouse prostate</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>For the library screening, CD-1 mice were anesthetized with Avertin (0.015 ml/g) and injected intravenously (tail vein) with phage libraries containing e9 transducing units diluted in 200 μl of DMEM. The phage was rescued from tissues by bacterial infection, and about 300 individual colonies were grown separately. </Brief_Description>
<BiopanningDataSet_Comments>The phage bound also to vasculature in the human prostate. The peptide displayed by the prostate-homing phage, SMSIARL, was synthesized and shown to inhibit the homing of the phage when co-injected into mice with the phage.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1637</BiopanningDataSetID>
<Peptides>CNLYSCLK
AREYRWLG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:11562257</Reference>
<Target_Name>Anti-phosphotyrosine monoclonal antibody PY20</Target_Name>
<Template_Name>Phosphotyrosine</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>pGWX3YX4 phage display library</Library_Name>
<Affinity_Measurement_Method>Western blot</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Among the randomly picked clones from pGWX3YX4, a band at 24.5 kD by Western blot, that corresponded to the gIII product containing the displayed peptide, was present in 2 clones CNLYSCLK and AREYRWLG, and it was absent from the control phage derived from the parent pGWg3 vector. This was proof that the displayed peptide was a Tie-2 substrate in the phage context.</Affinity_Measurement_Description>
<Brief_Description>The phage libraries were phosphorylated using a fusion protein of GST and human Tie-2 kinase domain (hGST-Tie-2).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1638</BiopanningDataSetID>
<Peptides>EAIVYVWGR
RLVAYEGWV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:11562257</Reference>
<Target_Name>Anti-phosphotyrosine monoclonal antibody PY20</Target_Name>
<Template_Name>Phosphotyrosine</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>pGWX4YX4 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Anti-phosphotyrosine ELISA of clones from pGWX4YX4 also identified 2 positive clones EAIVYVWGR and RLVAYEGWV with a signal over background &gt;2 (data not shown).</Affinity_Measurement_Description>
<Brief_Description>The phage libraries were phosphorylated using a fusion protein of GST and human Tie-2 kinase domain (hGST-Tie-2).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1639</BiopanningDataSetID>
<Peptides>LPLTPLP</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:17360703</Reference>
<Target_Name>Peptide  IDQYRMQRDKEFRLKQ</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>The most common phage sequence observed was LPLTPLP. When this sequence was used to search the human genome data base using the \&quot;short, nearly exact match\&quot; BLAST algorithm, an exact match of phage peptide amino acids 2-7 was found to amino acids 85-90 of the H(+)-ATPase subunit a4. This sequence is PLTPLP in a4 and PEVPFP in a1.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1640</BiopanningDataSetID>
<Peptides>WHWQRPLMPVSI(0.7)
WHWSPRTALYTT(0.05)
WHWNFKPPHDLL(0.06)
WHWKPPAPYVWW(0.12)</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:18363413</Reference>
<Target_Name>Trinitrotoluene, TNT</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 and Ph.D.-C7C phage display library pool</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>1641</BiopanningDataSetID>
<Peptides>HPNFSKYILHQR(0.24)
QRPTTQQGPSML(0.24)
QRPTTQLGSEYA(0.06)</Peptides>
<Motif></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:18363413</Reference>
<Target_Name>2,4-dinitrotoluene, DNT</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 and Ph.D.-C7C phage display library pool</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>1642</BiopanningDataSetID>
<Peptides>HVGGSSV
SLRGDGSSV
SVRGSGSGV
SVGSRV
SVVRDGSEV
SGRKVGSGSSV
SRKQGGTEV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18297085</Reference>
<Target_Name>Human lewis lung carcinoma, LLC</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>T7 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>1643</BiopanningDataSetID>
<Peptides>HVGGSSV
SLRGDGSSV
SVGSRV
SVVRDGSEV
SGRKVGSGSSV
SRKQGGTEV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18297085</Reference>
<Target_Name>Mouse GL261 glioblastoma</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>T7 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>1644</BiopanningDataSetID>
<Peptides>MSGDIISLAPTG
GPFFPKSLTTTS
NAPLSHIPENPR
SISAMPAPANSS
SVSVGMKPSPRP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18582017</Reference>
<Target_Name>Semiconductor GaN(0001) surface</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>As the abundance of the last sequence was 60%, hence revealing a high affinity for the test surface, the sequence SVSVGMKPSPRP was selected as the specific peptide for the GaN (0001) surface, denoted &quot;GaN_probe&quot; in the following. This sequence presents a hydrophobic first half and a hydrophilic second half.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1645</BiopanningDataSetID>
<Peptides>TDSILRSYDWTY(1)
TQQPLEGHQLPY(1)
TGVSWSVAQPSF(1)
SVSVGMKPSPRP(1)
SQWNSPPSSAAF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19137069</Reference>
<Target_Name>Non-small cell lung cancer (CL1-5)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The targeting phage TDSILRSYDWTY bound to several NSCLC cell lines but not to normal cells. Both the targeting phage and the synthetic peptide recognized the surgical specimens of NSCLC with a positive rate of 75% (27 of 36 specimens). In severe combined immunodeficiency (SCID) mice bearing NSCLC xenografts, the targeting phage specifically bound to tumor masses. The tumor homing ability of the targeting phage was inhibited by the cognate synthetic peptide, but not by a control or a WTY-mutated peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1646</BiopanningDataSetID>
<Peptides>TDSILRSYDWTY(20)
DMPKQLLAPWYY(2)
SYPLSFLGPLIS(1)</Peptides>
<Motif>W-[TY]-Y</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:19137069</Reference>
<Target_Name>Non-small cell lung cancer (CL1-5)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The targeting phage TDSILRSYDWTY bound to several NSCLC cell lines but not to normal cells. Both the targeting phage and the synthetic peptide recognized the surgical specimens of NSCLC with a positive rate of 75% (27 of 36 specimens). In severe combined immunodeficiency (SCID) mice bearing NSCLC xenografts, the targeting phage specifically bound to tumor masses. The tumor homing ability of the targeting phage was inhibited by the cognate synthetic peptide, but not by a control or a WTY-mutated peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1647</BiopanningDataSetID>
<Peptides>TDSILRSYDWTY(27)
DMPKQLLAPWYY(3)</Peptides>
<Motif>W-[TY]-Y</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:19137069</Reference>
<Target_Name>Non-small cell lung cancer (CL1-5)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The targeting phage TDSILRSYDWTY bound to several NSCLC cell lines but not to normal cells. Both the targeting phage and the synthetic peptide recognized the surgical specimens of NSCLC with a positive rate of 75% (27 of 36 specimens). In severe combined immunodeficiency (SCID) mice bearing NSCLC xenografts, the targeting phage specifically bound to tumor masses. The tumor homing ability of the targeting phage was inhibited by the cognate synthetic peptide, but not by a control or a WTY-mutated peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1648</BiopanningDataSetID>
<Peptides>CMLPHHGAC
CNPGFAQAC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1-3</Rounds_of_Panning>
<Reference>PMID:18271563</Reference>
<Target_Name>Hydroxyapatite, HA</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>After three biopanning rounds, 56 clones were selected (18 from first round, 19 each from second and third rounds) and characterized in terms of their physicochemical properties and binding affinity to HA. On the basis of immunofiuorescence microscopy assays, out of 56 clones, 12 were characterized as strong binders with a surface coverage higher than 40%, 28 were moderate binders with a coverage between 35% and 10%, and 16 were weak binders with a coverage lower than 7%. In addition, ELISA was used to confirm these results and the data obtained from both techniques were consistent. Statistical analysis of the binders after binding characterization revealed that 67% of the strong binders were selected in the third round of panning; likewise, 69% of the weak binders were selected in the first round of panning. These results showed that selection of strong-binding clones was favored in the additional panning rounds.The strongest binding clone (CMLPHHGAC, 75 + 5% binding) and a weak-binding clone (CNPGFAQAC, 3 + 2% binding) were chosen for subsequent solid-phase peptide synthesis and mineralization experiments.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1649</BiopanningDataSetID>
<Peptides>DRHSRIVILMPLAYP</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:11707616</Reference>
<Target_Name>Anti-AMA-1 monoclonal antibody 5G8</Target_Name>
<Template_Name>Apical membrane antigen 1</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>Selected clones after four rounds of panning were shown to bind to MAb5G8-coated ELISA plates, in a dose-dependent manner, whereas a clone containing a peptide isolated by panning the same library on an unrelated protein was unable to bind MAb5G8 even at 10e11 CFU/ml.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1650</BiopanningDataSetID>
<Peptides>SWGPFPF(4)
SWGPLPF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:10427007</Reference>
<Target_Name>Anti-DON monoclonal antibody 6F5</Target_Name>
<Template_Name>Mycotoxin deoxynivalenol, DON</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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The absorbance was measured at 450 nm (data not shown). In ELISA, five of phage isolates exhibited binding to mAb 6F5. In competitive ELISA, binding of phage clones SWGPFPF and SWGPLPF to immobilized mAB 6F5 was competitively inhibited by free DON.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Fifteen individual phage plaques from the fourth-round-selected phages were randomly isolated and used to infect E. coli ER2537 for phage reamplification. Each of the 15 phage isolates was tested to determine its binding to mAb 6F5 by ELISA. Five of these phage isolates exhibited binding to mAb 6F5.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>