<result><BiopanningDataSet><Item><BiopanningDataSetID>1276</BiopanningDataSetID>
<Peptides>QLETFSIKNMPR
TSIPHIMYLDPF
FKWPTTEWPSRL
NFMESLPRLGMH
SLTVPFLPLYVP
ASRQDMQNLAPP</Peptides>
<Motif>E-S-L-S-R-x(2)-M-x(2)-L-x-P</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:20619902</Reference>
<Target_Name>Anti-IL-2 monoclonal antibody 3A1</Target_Name>
<Template_Name>Interleukin-15</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>Bound phages were competitively eluted with recombinant goose IL-2.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1277</BiopanningDataSetID>
<Peptides>WAPGSMPTSRLA
HLPTSSLFDTTH
SHPWNAQRELSV
ATWSHHLSSAGL
DRYNSEWLPYSP
SSPHHMVSYTWL</Peptides>
<Motif>S-H(2)-L-P-T-S-x-L</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:20619902</Reference>
<Target_Name>Anti-IL-2 monoclonal antibody 3B3</Target_Name>
<Template_Name>Interleukin-15</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>Bound phages were competitively eluted with recombinant goose IL-2.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1278</BiopanningDataSetID>
<Peptides>VPVIWDVPYQSL
MHNPWDAFMEAS
GHPDPWLIEAPS
SHDPWDLLPLPY
MHPDPWDAPESR
YHSDPWSGFLKD
KPVYWDHELSKS</Peptides>
<Motif>H-P-D-P-W-D-A-P-L-S(2)</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:20619902</Reference>
<Target_Name>Anti-IL-2 monoclonal antibody 5A9</Target_Name>
<Template_Name>Interleukin-15</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>Bound phages were competitively eluted with recombinant goose IL-2.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1279</BiopanningDataSetID>
<Peptides>TLKPTQASLVHG
HVGTGDGHEHWQ
QLETFSIKNMPR
HSNWRVPSPWQL
GIHELNVARLRL</Peptides>
<Motif>H-E-P-W-Q-L-x-L</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:20619902</Reference>
<Target_Name>Anti-IL-2 monoclonal antibody 5C3</Target_Name>
<Template_Name>Interleukin-15</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>Bound phages were competitively eluted with recombinant goose IL-2.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1280</BiopanningDataSetID>
<Peptides>CFRHMTEQC(6)[0.545]
CIPLPFYNC(5)[0.22]
CSHLYLHNC(2)[0.464]
CPLTGTSKC(1)[1.04]
CTLKVRGEC(1)[0.97]
CGFWHTSKC(1)[0.411]
CAWPSKDNC(1)[0.887]
CIPLLFHNC(1)[0.893]
CWGAMVHPC(1)[0.452]
CHASLKHRC(1)[0.785]
CYTPWMPRC(1)[2.01]
CTYLAPKGC(1)[0.851]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19027991</Reference>
<Target_Name>Beta-amyloid protein 42 (Beta-APP42)</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>To determine the apparent dissociation constant (Kd, nM), the amyloid-beta 42 coated wells were incubated with twofold serial dilutions of each phage clone, starting with 1.0e12 virions(1.66e(-8) M) in the first well and ending with 8.0e6 virions (1.33e(-13) M) in the last well. Kd of the 12 selected clones displaying the highest affinities for amyloid-beta 42 was shown. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Two phage clones expressing the peptides C-IPLPFYN-C and C-FRHMTEQ-C were strongly selected because they are present in several copies. The first peptide is characterized by five hydrophobic amino acids out of seven suggesting that it interacts with Aβ42 by hydrophobic bonds. It is interesting to note that Aβ42 itself aggregates by hydrophobic mechanisms inside AP structures. On the other hand, peptide C-FRHMTEQ-C is hydrophilic, so the interaction mechanism should be differ ent and could involve the hydrophilic N-terminus domain of Aβ42.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1281</BiopanningDataSetID>
<Peptides>TSYTTSIFGPRA(1)
ILANDLTAPGPR(1)
NYMSALAITTSL(1)
KPANLTSTPWVP(1)
LLADTTHHRPWT(1)
ISMPVRPLLQDF(1)
SIVSTQTSLPLN(1)
SMTSHNQWHLLA(1)
ANPSPSTHHLTP(1)
TTTLLTATPHPH(1)
YPSFTHSATPSL(1)
FHQNSLRVHSSP(1)
QDVHLTQQSRYT(1)
NLNHERSQNLKM(1)
YESIRIGVAPSQ(1)
ERVMLPFPPAPW(2)
IPWTQHMAMSPM(1)
TNTSWMTAMTPF(1)
THTTNAEGYSPV(1)
TMGFTAPRFPHY(1)
SVSVGMKPSPRP(4)
SINGQWMRAIGK(1)
GIQLANPPRLYG(1)
QDMLKPYVDPLH(1)
SHHIPSYQWPLH(1)
WAETWPLAQRPP(1)
SNQTSDRPPLLT(1)
SSLEPWHRTTSR(2)
EWLAYDGIRAYS(1)
ETLPITLIARLT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>30</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20501662</Reference>
<Target_Name>Glycine receptor subunit alpha-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.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Human Embryonic Kidney (HEK) Cell were transfected with GlyR α1 subunit cDNA. Phage were applied to blank (control) HEK 293 cells. Then, phage that did not bind in this negative selection procedure were removed from the plate with a pipette, applied to the plate of GlyR-expressing cells.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1282</BiopanningDataSetID>
<Peptides>DHARYPWLRPPA
LPAFFVTNQTQD
YWNASPSASGVI
WHTEILKSYPHE
NSPRLVHTNTHN
LLADTTHHRPWT
SHVDDLGLRPLT</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20544195</Reference>
<Target_Name>Anti-EGFR monoclonal antibody 12H23</Target_Name>
<Template_Name>Epidermal growth factor receptor</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>Genomic DNA from 20 phage clones was sequenced, and seven different insert sequences were observed. Two (WHTEILKSYPHE and LPAFFVTNQTQD) mimotope candidates were  specifically recognized by the selecting antibody 12H23 but not by the isotype-matched control antibody.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1283</BiopanningDataSetID>
<Peptides>ASGALSPSRLDT(13)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20570932</Reference>
<Target_Name>Human 143B osteosarcoma cell lines</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>Before each selection round, a negative selection with the 293T human embryonic kidney cell line was done to subtract phages that bound to nontumor cells.</Brief_Description>
<BiopanningDataSet_Comments>After the final selection round, the ssDNAs of 20 clones were sequenced and analyzed. One sequence was found to be enriched in 65% of all sequenced clones. Peptide ASGALSPSRLDT shares a significant homology with heparinase II/III family protein, which binds and reacts with heparan sulfate proteoglycans.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1284</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(8)
NHNTSTWAAYST(1)
TLPSPHSLLTVH(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20329714</Reference>
<Target_Name>GaAs semi-insulating substrate</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 specific adhesion of these peptides is used for biofunctionalization of GaAs/AlGaAs photonic waveguides capable of enhancing the second harmonic generation response.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1285</BiopanningDataSetID>
<Peptides>YLCKFGC(1)
SPDELHK(2)
REPLVYW(1)
AEPIIYW(2)
KQPIVFW(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20844088</Reference>
<Target_Name>Anti-SEB monoclonal antibody ab53981</Target_Name>
<Template_Name>Enterotoxin type B (SEB)</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 N-terminal 15-mer peptide of SEB was determined to be an epitope of ab53981.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1286</BiopanningDataSetID>
<Peptides>MGGTLIASDQYQ(17)
QSLPASMSYQTA(1)
SLSASMDFMMYA(1)
NALRASNSFMDE(1)</Peptides>
<Motif>L-x(2)-S</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:20844088</Reference>
<Target_Name>Anti-SEB monoclonal antibody ab53981</Target_Name>
<Template_Name>Enterotoxin type B (SEB)</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 N-terminal 15-mer peptide of SEB was determined to be an epitope of ab53981.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1287</BiopanningDataSetID>
<Peptides>AHPWWLG(4)
SHPWYLG(2)</Peptides>
<Motif>P-x(2)-L-G</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-6</Rounds_of_Panning>
<Reference>PMID:20652782</Reference>
<Target_Name>Anti-S100A4 monoclonal antibody 22.3</Target_Name>
<Template_Name>Protein S100-A4</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 consensus sequence of MAb 22.3 mimotope was corresponded to amino acids 43-47 of S100A4 amino acid sequence.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1288</BiopanningDataSetID>
<Peptides>AWPDKQP(1)
SWPDKMP(1)
ILSDKMA(1)</Peptides>
<Motif>PDKQP</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4-6</Rounds_of_Panning>
<Reference>PMID:20652782</Reference>
<Target_Name>Anti-S100A4 monoclonal antibody 22.1</Target_Name>
<Template_Name>Protein S100-A4</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 consensus sequence of MAb 20.1 was corresponded to amino acid 94-98 of the C-terminal part of S100A4.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1289</BiopanningDataSetID>
<Peptides>HGINTTKPFKSV
WPSSYLSPIPYS
AVTTLTLVPAGT
ALTGSTKSAFGG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20405826</Reference>
<Target_Name>Na+ Montmorillonite (MMT)</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>1290</BiopanningDataSetID>
<Peptides>HGINTTKPFKSV
TSVRTHFPLYPV
GFEHKDQRFTRE</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20405826</Reference>
<Target_Name>Primary Ammonium C18 Modified Montmorillonite (MMT)</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>1291</BiopanningDataSetID>
<Peptides>HGINTTKPFKSV
GTFPLAIKARDP
LHLPSDRLRLWG
MHRSDLMSAAVR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20405826</Reference>
<Target_Name>Quaternary Ammonium C18 Modified Montmorillonite (MMT)</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>1292</BiopanningDataSetID>
<Peptides>LSVTYCFVY
NSIWGLFVH
PVNMTFVAL
RFSTYVSSW
VHFSYVSVV
RYSCARSTS
WYARFNLAA
WVRFVGVTG
GRWVALLDV
SVARFLVVD
RVRPARYLG
YVQVARYLS
RFLGMRRGF
VRWLAWKMV
LRYIMALAV
GTRFALETS
WDRWAMSTG
RYWVVIETV
SKGARFWLR
RWGFRFFAG
FSRYFSLRL
YSRWEVRFM
AWVRFWEDD
RYLEIADFK
LRVSFLDIA
FVSLWLEVA
AWGVYLDLG
WGVYLEAVS
YVTGYLDVV
GRVFFWDLE
MVGFWELVR
PPRGWKLEW
VSLYSSDGL
VVGYLMEVL
VSLFMGIDF
VYTRLEGCL
VVAFLMGQD
QGFLSFLRE
WAWLMATME
WIFYSLSTE
WVLPVQWSM
VGFLFNLLW
YVFRMRLVS
VVFLAAGSY
WLSLLNVRV
MIGYAVRPH
FWAFALARA
EPYMLGVTR
GTCYMSVVS
VRMMCWYPV
EARVLACLF</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>51</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20338912</Reference>
<Target_Name>Chymase</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>X9 T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Nonapeptide-coding inserts were then sequenced from 75 individually sampled phages. Fifty-one of the obtained sequences were aligned. Seventeen background sequences that had also been observed in analyses of other enzymes were excluded. Eleven of these contained the insert WCQVQSVCA and six the insert TLMVPRTGS. Four sequences contained stop codons. The remaining three sequences contained repetitive sequences and did not contain aromatic aa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1293</BiopanningDataSetID>
<Peptides>RLQLKL(2)
RTRYED(3)
RIPLEM(3)
QFDEPR(3)
TSAVRT(2)
QCTGRF(1)
ITDMAA(1)
WRPCES(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:20460372</Reference>
<Target_Name>Breast cancer tumors</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>pComb M13 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>1294</BiopanningDataSetID>
<Peptides>RLQLKL(11)
GLWQGP(7)
QCTGRF(5)
LPGMMG(5)
DVGTTE(5)
TDLGAM(5)
GMMYRS(4)
DSNAES(4)
ITDMAA(3)
RWRTNF(4)
WRPCES(2)
WRNTIA(3)
IDKQLE(3)
FMEIET(3)
HEVVAG(2)
GGHTRQ(2)
INGKVT(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>17</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20460372</Reference>
<Target_Name>Mixed liver/kidney tissue extracts</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>pComb M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Phage library was pre-exposed to extracts of liver and kidney, tissues that typically have high nonspecific uptake of drugs and imaging agent, to allow cleavage by proteases contained within these extracts. Isolated phage were reamplified and subjected to six additional rounds of both negative (no liver/kidney cleavage) and positive (tumor cleavage) selection, with representative phage being isolated and sequenced after each round.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1295</BiopanningDataSetID>
<Peptides>QQSWPIS(4)</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:20648291</Reference>
<Target_Name>Pd wire</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>Peptide QQSWPIS appeared four times among ten colonies. The peptide can bind to the Pd NC surface and act as a stabilizer to mediate Pd crystal nucleation and growth.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1296</BiopanningDataSetID>
<Peptides>MFQRMAVDA(1)
YRQMSAPTL(1)
WFGQLQAAQ(1)
YRHAQAYGV(1)
MPRQYTQMI(1)
FHKVYRGLL(1)
WQMAMSRHL(1)
SIMMMGAVR(1)
WYTLLKSRL(1)
YKPMLASVG(1)
YAAMRGGQI(1)
YKPLWGQMT(1)
NYQMMGTMR(1)
FERARSRLL(1)
YLRMLQILK(1)
NWRALRGAL(1)
YRQMWVNRA(1)
FMAMRAVRL(1)
FTMLMNQVM(1)
VYRAQGPQM(1)
MMSRMLGQT(1)
SSGRYARLG(1)
TFYRMGTQM(1)
WIGQMYAAK(1)
YRMQSNHVS(1)
DRSMEWRMM(1)
FSAIRNRIL(1)
YRAMQTTLS(1)
NYLGMKPRV(1)
RGFRHMMAA(1)
YQQMGARLM(1)
SWRHIQTRV(1)
MYGLMLAQR(1)
YQALRAYWQ(1)
RFTQMMAVA(1)
WKGLQGALS(1)
FMRLGGGHL(1)
IWHMQNARV(1)
YKLLRATQM(1)
LWQSFMQMA(1)
FHQLRGGSL(1)
YRGMQRRTL(1)
YGKLRGGTL(1)
QVGKYLGLG(1)
TYRGMAGFR(1)
RVFQNLRAS(1)
WRQMYRAQL(1)
RSYSLAPGR(1)
TWNSLRGRL(1)
QRYNAMRAA(1)
YIMQMNRVV(1)
LTLMQAKRL(1)
RFTQMGALA(1)
YYGKMPALV(1)
PWQAMRGWL(1)
KKIMSYHAL(1)
YRGMSAFRA(1)
MFHRMSGLQ(1)
GQRSYSSMQ(1)
YMMQKSVRA(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>60</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:1402647</Reference>
<Target_Name>HLA class II histocompatibility antigen, DRB1-1 beta chain</Target_Name>
<Template_Name>HLA class II histocompatibility antigen, DM</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>M13lib X9 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>DR1 molecules were isolated from the human EBV-B cell line, HOM-2. M13 phages were incubated with biotinylated DR1 in binding buffer (50 mM Tris-C1, pH 7.5, 150 mM NaC1, 1 mM EDTA, 1 mM PMSF, and 0.2% NP-40). After at least 24 h incubation at room temperature, BSA-blocked streptavidin on 4% beaded agarose was added and incubated for 10 min. The M13 phage/DR1 complexes were purified by washing the solid phase several times with binding buffer.</Brief_Description>
<BiopanningDataSet_Comments>Competition experiments with both isolated phages and corresponding synthetic peptides showed that the binding was specific.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1297</BiopanningDataSetID>
<Peptides>EPLQLKM
QQQLSTH</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:20942387</Reference>
<Target_Name>TIMREX SLP30 Primary Synthetic Potato graphite</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>Modification of graphene with bifunctional peptides reveals both the ability to impart selective recognition of gold nanoparticles and the development of an ultrasensitive graphene-based TNT sensor.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1298</BiopanningDataSetID>
<Peptides>TMGFTAPRFPHY
YHRMPQALSAME</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:20942387</Reference>
<Target_Name>TIMREX SLP30 Primary Synthetic Potato graphite</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>Modification of graphene with bifunctional peptides reveals both the ability to impart selective recognition of gold nanoparticles and the development of an ultrasensitive graphene-based TNT sensor.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1299</BiopanningDataSetID>
<Peptides>GAMHLPWHMGTL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20942387</Reference>
<Target_Name>AFM standard highly ordered pyrolytic graphite (HOPG)</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>Modification of graphene with bifunctional peptides reveals both the ability to impart selective recognition of gold nanoparticles and the development of an ultrasensitive graphene-based TNT sensor.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1300</BiopanningDataSetID>
<Peptides>GAMHLPWHMGTL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:20942387</Reference>
<Target_Name>N006 nano graphene platelets</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>Modification of graphene with bifunctional peptides reveals both the ability to impart selective recognition of gold nanoparticles and the development of an ultrasensitive graphene-based TNT sensor.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>