<result><BiopanningDataSet><Item><BiopanningDataSetID>2751</BiopanningDataSetID>
<Peptides>CRGDKGPDC(0.152)
CRGDRGPDC(0.091)
CRGDKGPEC(0.061)
CRGDKTTNC(0.03)
CRGDHAGDC(0.061)
CRGDHGVEC(0.03)
CGRGDNLPC(0.03)
CGRGDNLAC(0.03)
CEKRGDNLC(0.03)
CEKRGDSVC(0.061)
CSGRGDSLC(0.03)
CGKRGDSIC(0.03)
CTGRGDALC(0.03)
CRGDSAC(0.03)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:19962669</Reference>
<Target_Name>Prostate cancer bone metastasis cell</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 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>2752</BiopanningDataSetID>
<Peptides>CRGDKGPDC(0.136)
CRGDKGENC(0.045)
CGRGDSPDC(0.045)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:19962669</Reference>
<Target_Name>Prostate cancer bone metastasis cell</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 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>2753</BiopanningDataSetID>
<Peptides>CRGDKGPEC(0.10)
CRGDKHADC(0.05)
CRGDHAANC(0.05)
CRGDAGINC(0.05)
CGRGDMPSC(0.05)
CEKRGDSLC(0.05)</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:19962669</Reference>
<Target_Name>Prostate cancer bone metastasis cell</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 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>2754</BiopanningDataSetID>
<Peptides>LLADTTHHRPWT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20621144</Reference>
<Target_Name>Heart muscle of mdx mouse</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>In the first round, mdx mice were injected with 2e11 phage particles in PBS each via tail vein injection under anesthesia and sacrificed 2 h later. The heart was harvested. The phage particles homing to the heart muscle were harvested. For round 2 and 3 of the selection, 2e10 and 2e9 phage harvested from the heart muscle was injected into mdx mice respectively. For the last selection, heart tissue was also taken and phage within were amplified.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2755</BiopanningDataSetID>
<Peptides>LLADTTHHRPWT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20621144</Reference>
<Target_Name>Heart muscle and liver of mdx mouse</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>In the first round, mdx mice were injected with 2e11 phage particles in PBS each via tail vein injection under anesthesia and sacrificed 2 h later. The heart was harvested. The phage particles homing to the heart muscle were harvested. For round 2 and 3 of the selection, 2e10 and 2e9 phage harvested from the heart muscle was injected into mdx mice respectively. For the last selection, liver tissue was also taken and phage within were amplified.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2756</BiopanningDataSetID>
<Peptides>KPANLTSTPWVP(1)
TNAPPANMPFRS(1)
SEIGMVHRSHQW(1)
WSPGQQRLHNST(1)
FSPLHTSTYRPS(1)
IVHPSTM(1)
SKTFNTHPQSTP(1)
GFAKSHPMSLPS(1)
GFPKSHPMSLP(1)
APFKVPSLPSNT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20621144</Reference>
<Target_Name>Quadriceps muscle of mdx mouse</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>In the first round, mdx mice were injected with 2e11 phage particles in PBS each via tail vein injection under anesthesia and sacrificed 2 h later. The quadriceps was harvested. The phage particles homing to the quadriceps muscle were harvested. For round 2 and 3 of the selection, 2e10 and 2e9 phage harvested from the quadriceps muscle was injected into mdx mice respectively. For the last selection, quadriceps tissue was also taken and phage within were amplified.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2757</BiopanningDataSetID>
<Peptides>KPANLTSTPWVP(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20621144</Reference>
<Target_Name>Quadriceps muscle and liver of mdx mouse</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>In the first round, mdx mice were injected with 2e11 phage particles in PBS each via tail vein injection under anesthesia and sacrificed 2 h later. The quadriceps was harvested. The phage particles homing to the quadriceps heart were harvested. For round 2 and 3 of the selection, 2e10 and 2e9 phage harvested from the quadriceps muscle was injected into mdx mice respectively. For the last selection, liver tissue was also taken and phage within were amplified.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2758</BiopanningDataSetID>
<Peptides>CPLLYSWWC(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:16312021</Reference>
<Target_Name>Prostate-specific antigen</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>The binding of the anti-total PSA mAb 8F8G5 to PSA was found to enhance the enzymatic activity of the bound PSA. Therefore the library was screened with PSA immobilized into microtiter wells coated with anti-total PSA mAb 8F8G5.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-seven different sequences were obtained, but only one clone, obtained nine times, gave a strong positive signal with PSA presented by 8G8F5. This clone (CPLLYSWWC) did not react with either PSA, PSA-ACTor 8G8F5 alone. Moreover, CPLLYSWWC reacted also strongly with PSA presented by 11E5C6 whereas its binding to PSA presented by anti-total PSA mAb 5D5A5 was moderate.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2759</BiopanningDataSetID>
<Peptides>QYLSPLVTQWEW(5)</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:16312021</Reference>
<Target_Name>Prostate-specific antigen</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 dodecapeptide library was screened with PSA immobilized into microplate wells coated with anti-total PSA mAb 11E5C6.</Brief_Description>
<BiopanningDataSet_Comments>After three biopannings, 36 clones were randomly isolated and their DNA was sequenced. The deduced amino acid sequences of the corresponding inserts identified 22 different sequences. When tested in ELISA, these different clones did not recognize PSA or PSA-ACT coated directly in the wells. However, one clone (QYLSPLVTQWEW) obtained recognized specifically either PSA or PSA-ACT presented by either 11E5C6 or 8G8F5 but not 5D5A5.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2760</BiopanningDataSetID>
<Peptides>ACGWHPQNACG(17)
ACTWHPQVGCG(2)
ACNWHPQFSCG(1)
ACEWHPQSGCG(1)
ACVWHPQVPCG(1)
ACQWHPQNGCG(1)
ACSWHPQAACG(1)
ACGYHPQQGCG(1)
ACYHPQGDYCG(1)
ACSVPMQIYCG(1)
ACSVPVQVFCG(1)
ACSAPGGSLCG(1)
ACSAPTGSLCG(1)
VCPGHATNSCG(1)</Peptides>
<Motif>HPQ</Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The CX7C phage library cyclized with BSBBA was subjected to two consecutive selection rounds against streptavidin as follows. The population was first depleted of trans binders by adding and discarding 7 times 10 μL magnetic streptavidin beads. The remaining phage were exposed 5 min to the UV light and incubated with 20 μL magnetic streptavidin beads to capture cis binders. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2761</BiopanningDataSetID>
<Peptides>ACHPQGDLYCG(9)
ACHPQGDGICG(4)
ACHPQGDGVCG(2)
ACHPQGDVDCG(1)
ACHPQGDQVCG(1)
ACHPQGEMNCG(1)
ACHPQGPASCG(1)
ACHPQNDSDCG(1)
ACHPQNDKNCG(1)
ACHPQNDIFCG(1)
ACHPQNNRYCG(1)
ACHPQFWSSCG(1)
ACHPQFHPDCG(1)
ACSSPLPQFCG(1)
ACSSPDVQVCG(1)
ACSSPDRDHCG(1)
ACSFFGAPKCG(1)
ACPAHPDKGCG(1)
ACHPMAPANCG(1)</Peptides>
<Motif>HPQ</Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The phage-peptides were not cyclized with BSBBA and exposed to UV light. The population was first depleted of trans binders by adding and discarding 7 times 10 μL magnetic streptavidin beads. The remaining phage were exposed 5 min to the UV light and incubated with 20 μL magnetic streptavidin beads to capture cis binders. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2762</BiopanningDataSetID>
<Peptides>AWCHPQGGCLG(5)
AGCHPQGPCQG(4)
ATCHPQVPCRG(4)
AKCHPQVPCKG(3)
AGCFLVWACQG(2)
AGCWGQWACQG(2)
AMCHHPQNCVG(1)
ASCWHPQFCGG(1)
AYCVHPQFCRG(1)</Peptides>
<Motif>HPQ</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>AXCX5CXG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The XCX5CX phage library cyclized with BSBBA was subjected to two consecutive selection rounds against streptavidin as follows. The population was first depleted of trans binders by adding and discarding 7 times 10 μL magnetic streptavidin beads. The remaining phage were exposed 5 min to the UV light and incubated with 20 μL magnetic streptavidin beads to capture cis binders. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2763</BiopanningDataSetID>
<Peptides>AGCHPQGPCQG(12)
AKCHPQVPCKG(4)
ATCHPQVPCRG(4)
APCHPQVPCQG(1)
AYCHPQVGCWG(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>AXCX5CXG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The phage-peptides were not cyclized with BSBBA and exposed to UV light. The population was first depleted of trans binders by adding and discarding 7 times 10 μL magnetic streptavidin beads. The remaining phage were exposed 5 min to the UV light and incubated with 20 μL magnetic streptavidin beads to capture cis binders. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2764</BiopanningDataSetID>
<Peptides>ASCFPSFFCNG(6)
AGCWQAWTCVG(5)
AGCWGQWACQG(4)
ASCFPRWVCGG(3)
AWCSHPQNCIG(2)
AYCGHPQNCWG(1)
ASCFPVLACIG(1)
ASCFPMLFCVG(1)
AFCMLRWTCQG(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>AXCX5CXG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The negative selection for depletion of trans binders was omitted. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2765</BiopanningDataSetID>
<Peptides>AGCHPQGPCQG(10)
ATCHPQVPCRG(5)
AKCHPQVPCKG(3)
ARCHPQGPCQG(1)
AECHPQAPCTG(1)
AACHPQAPCRG(1)
AHCHPQAPCRG(1)
ASCHPQVPCQG(1)
AYCHPQVGCWG(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24702159</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,1X2R,2DYH,2NR6,1ILP,1ILQ,2XDF,3EZA,3EZB,3EZE,2XDF,3MJG,1J7V,1Y6K,3RY6,4K0V ,3QD6,1QTY,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>AXCX5CXG phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The phage-peptides were not cyclized with BSBBA and exposed to UV light. The negative selection for depletion of trans binders was omitted. Binders were eluted by addition of biotin and buffer with a low pH.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2766</BiopanningDataSetID>
<Peptides>MEWSLEKGYTIK(24/66)
WGWSLSHGYQVK(5/66)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:24859530</Reference>
<Target_Name>Granulocytic myeloid-derived suppressor cells, granulocytic MDSCs</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>After the third round of biopanning, predominant MDSC-binding peptides were identified by PCR analysis of 66 individual phages eluted from granulocytic MDSCs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2767</BiopanningDataSetID>
<Peptides>MEWSLEKGYTIK(25/48)
WGWSLSHGYQVK(10/48)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:24859530</Reference>
<Target_Name>Monocytic myeloid-derived suppressor cells, monocytic MDSCs</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>After the third round of biopanning, predominant MDSC-binding peptides were identified by PCR analysis of 48 individual phages eluted from monocytic MDSCs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2768</BiopanningDataSetID>
<Peptides>HPWIPKR
WPWQHHR
WPWHHVR
WPWHNHR</Peptides>
<Motif>W-P-W-x(3)-R</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:24573486</Reference>
<Target_Name>Envelope glycoprotein E2(661)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Twenty-five randomly selected phages from the third round of biopanning bound to HCV E2661. Four clones (HPWIPKR, WPWQHHR, WPWHHVR, WPWHNHR) had higher affinities for binding HCV E2661 protein compared to the other clones.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2769</BiopanningDataSetID>
<Peptides>SHSEFWDWGP[3.69 ± 0.11, 1.6]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:25014588</Reference>
<Target_Name>Histone demethylase KDM1A</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>X7+X12+CX7C M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In direct phage ELISA, absorbance values were measured at 490nm. Absorbances of the peptide were 0.28 ± 0.03, 0.06 ± 0.01 and 0.05 ± 0.01 when GST, BSA and skim milk acted as control target. Besides, competitive ELISA experiments were performed between free and surface-immobilized KDM protein for phage binding. And apparent EC50 values (μM) were determined by competition assay from triplicate analyses.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2770</BiopanningDataSetID>
<Peptides>AWDVIWDQLLQH[3.68 ± 0.07, 10]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:25014588</Reference>
<Target_Name>Histone demethylase KDM1B</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>X7+X12+CX7C M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In direct phage ELISA, absorbance values were measured at 490nm. Absorbances of the peptide were  0.12 ± 0.03, 0.08 ± 0.01 and 0.07 ± 0.02 when GST, BSA and skim milk acted as control target. Besides, competitive ELISA experiments were performed between free and surface-immobilized KDM protein for phage binding. And apparent EC50 values (μM) were determined by competition assay from triplicate analyses.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2771</BiopanningDataSetID>
<Peptides>GRMDWLGWRYEL[2.09 ± 0.14, 11]
SHSMSNRAPSALVRI[0.56 ± 0.06, 3.4]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:25014588</Reference>
<Target_Name>Histone demethylase KDM4A</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>X7+X12+CX7C M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In direct phage ELISA, absorbance values were measured at 490nm. Absorbances of GRMDWLGWRYEL were 0.05 ± 0.00, 0.05 ± 0.01 and 0.05 ± 0.02, and that of SHSMSNRAPSALVRI were 0.05 ± 0.01, 0.08 ± 0.02 and 0.08 ± 0.01 when GST, BSA and skim milk acted as control target. Besides, competitive ELISA experiments were performed between free and surface-immobilized KDM protein for phage binding. And apparent EC50 values (μM) were determined by competition assay from triplicate analyses.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2772</BiopanningDataSetID>
<Peptides>CKWMDDGYC[0.27 ± 0.06, 56]
CYTRNMNQC[1.89 ± 0.14, 1.3]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-5</Rounds_of_Panning>
<Reference>PMID:25014588</Reference>
<Target_Name>Histone demethylase KDM4C</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>X7+X12+CX7C M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In direct phage ELISA, absorbance values were measured at 490nm. Absorbances of CKWMDDGYC were 0.07 ± 0.02, 0.05 ± 0.01 and 0.04 ± 0.01, while that of CYTRNMNQC were 0.12 ± 0.03, 0.07 ± 0.02 and 0.06 ± 0.02 when GST, BSA and skim milk acted as control target. Besides, competitive ELISA experiments were performed between free and surface-immobilized KDM protein for phage binding. And apparent EC50 values (μM) were determined by competition assay from triplicate analyses.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2773</BiopanningDataSetID>
<Peptides>MYPWTEPSYLSN(16)[3.67 ± 0.40]
SPWTEPHYMAEP(3)[3.07 ± 0.91]
TPWTERWYWTSP(3)[3.43 ± 0.35]</Peptides>
<Motif>P-W-T-E-x(2)-Y</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:25048232</Reference>
<Target_Name>Human brain-seeking breast carcinoma 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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The bound peptide-phage clones were detected by phage cell-binding ELISA. ELISA. Wild-type M13 phage (Insertless-M13) lacking the peptide insert served as a negative control. The relative binding affinity positive-to-negative (P/N) ratios of peptide-phage clones to 231-BR cells are computated as means ± SD. </Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>M13 phage clone displaying MYPWTEPSYLSN sequence, specifically bound to 231-BR cells and the binding could be competitively abolished by the peptide MYPWTEPSYLSN. Thus, this peptide is a promising peptide binding to human brain metastatic breast cancer.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2774</BiopanningDataSetID>
<Peptides>CSHMEYPRC[2 ± 0.14]
CESAYMNNC[1.86 ± 0.02]
CTVRTSADC[1.88 ± 0.13]
CNCDYVLTC[1.87 ± 0.14]
CLMRTNDQC[1.75 ± 0.29]
CLKADKAKC[1.46 ± 0.03]
CGFQHIGNC[1.24 ± 0.05]
CVHVAQGRC[1.14 ± 0.09]
CLPMTKHVC[1.13 ± 0.1]
CPIKDLLAC[1.14 ± 0.12]
CLKLGEKWC[0.74 ± 0.15]
CNLCPTYYC[0.5 ± 0.02]</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:25058570</Reference>
<Target_Name>Human breast cancer cell line MDA-MB-231</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>Phage binding to MDA-MB-231 cells was detected by cellular ELISA. Phage lacking an insert was used as the negative control. The experiments were performed in triplicate, and results are mean ± SD average OD450 nm values. The OD450 nm value of negative control phage binding to MDA-MB-231 cells was 0.23 ± 0.04. Data shown were reproduced from Fig. 1 in the reference.</Affinity_Measurement_Description>
<Brief_Description>Screening of the phage library was performed by the BRASIL method, which allows the separation of cell-bound from unbound phage in one step.</Brief_Description>
<BiopanningDataSet_Comments>Single-photon emission CT (SPECT) and near-infrared fluorescence (NIRF) imaging showed enrichment of peptide CLKADKAKC to the xenograft tumors in nude mice. It could be used for breast cancer molecular imaging, which may represent a new avenue for breast cancer diagnostics, staging and assessments of therapeutic response.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2775</BiopanningDataSetID>
<Peptides>CNLSSSWIC(24/47)[0.669 ± 0.007]
CPSTLGASC(7/47)[0.632 ± 0.01]
CVPRLSAPC(7/47)[0.6 ± 0.003]
CVATLPAGC(5/47)[0.476 ± 0.007]
CHPLRSAFC(3/47)[NT]
CSHTSLESC(1/47)[NT]</Peptides>
<Motif></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:25078431</Reference>
<Target_Name>Myoglobin</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>The binding activity of the first four selected phage clones to myoglobin coated on plates was determined by phage binding ELISA. Data shown were optical density (OD) at 490 nm and reproduced from Fig. 4 in the reference. Phage library was used as a control phage, which had the value of 0.077 ± 0.008 when binding to the myoglobin.</Affinity_Measurement_Description>
<Brief_Description>Each biopanning round consists of negative selection or sub-traction of phages that nonspecifically binds to the Dynabeads and subsequent positive selection of phages that binds to myoglobin. In the negative selection, phage library in PBS was added to the BSA-blocked Dynabeads and incubated to subtract the phages that binds to the beads.</Brief_Description>
<BiopanningDataSet_Comments>Forty seven phage clones were randomly picked from phage clones of the third, fourth, and fifth round. Four phage clones(CNLSSSWIC, CPSTLGASC, CVPRLSAPC, CVATLPAGC) from the third round of biopanning had higher frequency. The analysis of binding affinity showed that the peptide CPSTLGASC had higher binding affinity (Kd= 57 nM) than did the CNLSSSWIC and CVPRLSAPC peptide (Kd= 125 nM and 293 nM, respectively). Cross binding activity to other proteins, such as bovine serum albumin, troponin I, and creatine kinase-MB, was minimal. The identified peptides can be used for the detection of myoglobin and may be a cost effective alternative to antibodies.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>