<result><BiopanningDataSet><Item><BiopanningDataSetID>1726</BiopanningDataSetID>
<Peptides>TTAAVDMPRSTP(3)
HESFWYLPHQSY(1)
LLADTTHHRPWT(8)
QSNYPRASYVFQ(1)
KSLSRHDHIHHH(2)
MPWAHRAPQGIA(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>DOI:10.1021/cm071515t</Reference>
<Target_Name>(001)-oriented TiO2</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>A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. A additional round of screening were conducted with a 0.5% TBST wash solution (for a total of six rounds of biopanning).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1727</BiopanningDataSetID>
<Peptides>LLADTTHHRPWT(2)
SHAFTASPRYLH(4)
KSLSRHDHIHHH(6)
YAKSPPTPYYTP(4)
LAPKPFEPRYTR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>7</Rounds_of_Panning>
<Reference>DOI:10.1021/cm071515t</Reference>
<Target_Name>(001)-oriented TiO2</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>A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. Two additional rounds of screening were conducted with a 0.5% TBST wash solution (for a total of seven rounds of biopanning).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1728</BiopanningDataSetID>
<Peptides>KSLSRHDHIHHH(17)
SRPSRQPSASPT(3)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>8</Rounds_of_Panning>
<Reference>DOI:10.1021/cm071515t</Reference>
<Target_Name>(001)-oriented TiO2</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>A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. Three additional rounds of screening were conducted with a 0.5% TBST wash solution (for a total of eight rounds of biopanning).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1729</BiopanningDataSetID>
<Peptides>DPIYALSWSGMA(1)
TMATYVNQSLTG(1)
SVSLPYANLATH(1)
SLYNTAASHVPT(1)
DLNTNRTGMVLH(2)
NYLHNHPYGTVG(1)
LTPTSRPTPYPA(1)
KSLSRHDHIHHH(9)
NFRPVTAMPRLD(1)
NINANAAQIKRH(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>DOI:10.1021/cm071515t</Reference>
<Target_Name>(001)-oriented TiO2</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>A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. A additional round of screening were conducted with a 0.8% TBST wash solution (for a total of six rounds of biopanning).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1730</BiopanningDataSetID>
<Peptides>TQHLSHPRYATK(9)
YAKSPPTPYYTP(8)
KSLSRHDHIHHH(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>7</Rounds_of_Panning>
<Reference>DOI:10.1021/cm071515t</Reference>
<Target_Name>(001)-oriented TiO2</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>A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. Two additional rounds of screening were conducted with a 0.8% TBST wash solution (for a total of six rounds of biopanning).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1731</BiopanningDataSetID>
<Peptides>APPGHHHWHIHH
MSASSYASFSWS
KPSHHHHHTGAN</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:12908327</Reference>
<Target_Name>Silica, Si</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>1732</BiopanningDataSetID>
<Peptides>MSPHPHPRHHHT
MSPHHMHHSHGH
LPHHHHLHTKLP
APHHHHPHHLSR
RGRRRRLSCRLL</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:12908327</Reference>
<Target_Name>Silica, Si</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>1733</BiopanningDataSetID>
<Peptides>LKAHLPPSRLPS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:16601154</Reference>
<Target_Name>Gold</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 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>1734</BiopanningDataSetID>
<Peptides>RKLPDAPGMHTW(34)
LDTTNVSGPMSS(1)
SYRLPVYLHALL(1)
SDPNQDWRRTTP(1)
LPSQLLSQVNLT(1)
LCANNTTSVHPP(1)
MQMEGKPTLTLR(1)
STLKNPINLLAN(2)
QDMIRTSALMLQ(1)
SCHVWYDSCSSP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:14624545</Reference>
<Target_Name>Titanium, Ti</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 three rounds of panning procedures carried out against Ti particles, we observed that 33 of 43 phages displayed on their surfaces peptides having the identical sequence.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1735</BiopanningDataSetID>
<Peptides>NFMSLPRLGHMH
TSNAVHPTLRHL</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:19422199</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.-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>Both peptide sequences possessed basic pI values; however, the peptide TSNAVHPTLRHL sequence possessed more basic and hydroxyl-containing residues, comparatively. Additionally, theoretical modeling of the peptide Pd surface binding capabilities suggests that the two histidine residues bind to the materials surface in a pinched arrangement, which will likely lead to open interaction sites between the solution and the metallic surface.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1736</BiopanningDataSetID>
<Peptides>TGTSVLIATPYV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:20083240</Reference>
<Target_Name>Gold</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>Metallic gold powder in an Eppendorf tube was directly used as the target material for isolation of binding phages instead of a substrate coated with the target material or a solution of phage with a target attached by affinity tags.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1737</BiopanningDataSetID>
<Peptides>LNAAVPFTMAGS</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:20627315</Reference>
<Target_Name>Titanium dioxide, TiO2</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>First, three rounds of phage display selection were performed in an Eppendorf PP tube containing a 5-mm-diameter and 2 mm amorphous-TiO2-coated disk. Secondly, an additional round of selection was performed on newly shaped surfaces.</Brief_Description>
<BiopanningDataSet_Comments>The TiO2-binding peptide sequence (LNAAVPFTMAGS) occurred in 50% of the clones.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1738</BiopanningDataSetID>
<Peptides>MTWDPSLASPRS</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:20627315</Reference>
<Target_Name>Stainless steel</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>First, three rounds of phage display selection were performed in an Eppendorf PP tube containing a 5-mm-diameter and 2 mm thick stainless steel. Secondly, an additional round of selection was performed on newly shaped surfaces.</Brief_Description>
<BiopanningDataSet_Comments>The stainless steel-binding peptide sequence (MTWDPSLASPRS) occurred in 70% of the clones.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1739</BiopanningDataSetID>
<Peptides>YQLRPNAESLRF</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:20627315</Reference>
<Target_Name>Bulk steel (edges)</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>A dominant peptide sequence for recognition of the steel of the edges was highlighted (YQLRPNAESLRF).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1740</BiopanningDataSetID>
<Peptides>AGETQQAM</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:20383127</Reference>
<Target_Name>Iridium oxide, IrO2</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>X8 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>1741</BiopanningDataSetID>
<Peptides>MFLRAG
LHADVW
QLYMKG
WAMSEV
EPGLDR
SFNILR
PVQASP
DSASHS
SPCRGL
GWWPHR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:7892246</Reference>
<Target_Name>Capsid protein</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>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The library had been incubated with a buffer containing BSA, before panning, to eliminate phage that bind BSA. The phage library was screened against truncated HBcAg (aa 3-148). The washing buffer used during affinity purification contained 0.15M NaCl.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1742</BiopanningDataSetID>
<Peptides>LLGRMK(15)[0.17 ± 0.01, 0.22 ± 0.01]
YLLRFR(11)[1.53 ± 0.10, ND]
LLGRLK(6)[1.13 ± 0.05, ND]
LLGRFK(2)[0.64 ± 0.03, ND]
LLGRFR(2)[NT]
LLGRLR(1)[NT]
LLGRMR(1)[NT]
SLWKWK(1)[NT]
WTFLRG(1)[NT]</Peptides>
<Motif>L-L-G-R-[MFL]-[KR]</Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:7892246</Reference>
<Target_Name>Capsid protein</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>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Relative dissociation constants (KdRel, μM) of the phage-truncated HBcAg complexes and the phage-full-length HBcAg complexes were shown, respectively. ND represents not determined. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>The library had been incubated with a buffer containing BSA, before panning, to eliminate phage that bind BSA. The phage library was screened against truncated HBcAg (aa 3-148). The washing buffer used during affinity purification contained 0.5M NaCl. In the first round of panning, 0.001% of phage bound to the membrane and this binding increased to 1% in the third panning.</Brief_Description>
<BiopanningDataSet_Comments>Of 46 independent clones, the sequence LLGRMK predominated. Six sequences are considered unrelated and not given in the original paper. LLGRMK-bearing phage bound to full-length HBcAg (aa 3-183) as efficiently as to truncated HBcAg but did not bind to heat-denatured, truncated HBcAg. The sequence LLGRMK could represent one loop of the binding site of an antibody to HBcAg, but more interestingly it may resemble a region of the HBsAg polypeptide that contacts the nucleocapsid in the intact virion.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1743</BiopanningDataSetID>
<Peptides>ANGCCD
HAILNI
ESQSVL
RVADIV
SKGTVA
DVSIGV
RYLVLE
NINSPV
IWLSNG
WPRGAG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:7892246</Reference>
<Target_Name>Bovine serum albumin (BSA)</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>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The library had been incubated with a buffer containing BSA, before panning, to eliminate phage that bind BSA. Thus, the peptides here are considered to be random sequences.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1744</BiopanningDataSetID>
<Peptides>CFDYAPYVSAVDDIC
LSAVDDLATVVYGSR
AGCTALSAVDDVPGC
ASSAVDDAPWAVITF
VGLLSVEELVPGGAA
GSFSAEHFLDDFAIW
RNVPPIFNDVYWLAF
GGVSAVPFMDYFPSW</Peptides>
<Motif>[ST]-A-V-D-D, S-A-V-P-x(2)-D, S-A-x(4)-D</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2-4</Rounds_of_Panning>
<Reference>PMID:10456916</Reference>
<Target_Name>Anti-RESA monoclonal antibody MAb 18/2</Target_Name>
<Template_Name>Ring-infected erythrocyte surface antigen</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f3-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Most phage isolated from this library bound to MAb 18/2-coated ELISA plates. The binding of representative peptides, CFDYAPYVSAVDDIC and GSFSAEHFLDDFAIW, to MAb 18/2 has been confirmed.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1745</BiopanningDataSetID>
<Peptides>QTAVDDAEAAAKCRHCI
QDETRSAVDSIPQAHCS
GLKNCTVQPWDATDVCD
QISAVS
LPAQPNACWPTMTPLCA
YVGSQSEDRDMSCGHCS
QQNDLLVYSAVPLSDCK
ASAAEGDD</Peptides>
<Motif>[ST]-A-V-D-D, S-A-V-P-x(2)-D, S-A-x(4)-D</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2-4</Rounds_of_Panning>
<Reference>PMID:10456916</Reference>
<Target_Name>Anti-RESA monoclonal antibody MAb 18/2</Target_Name>
<Template_Name>Ring-infected erythrocyte surface antigen</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X15CX phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Interestingly, sequences of two peptides QISAVS and ASAAEGDD align with the second motif only if the phage protein backbone of gpVIII to which the peptides are fused is considered to contribute to the binding. Most phage isolated from this library bound to MAb 18/2-coated ELISA plates. In contrast, phage lacking a peptide (wild-type M13 phage) did not bind to MAb 18/2, and one phage clone with the insert sequence YVGSQSEDRDMSCGHCS, which lacks the consensus motif, also did not bind. RESA protein inhibits binding of MAb 18/2 to selected phage. The binding of a representative peptide, GLKNCTVQPWDATDVCD, to MAb 18/2 has been confirmed.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1746</BiopanningDataSetID>
<Peptides>LWVGGGRNA(6)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:10867191</Reference>
<Target_Name>Grass carp hemorrhage virus</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 fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>To remove weakly or nonspecifically bound peptidea??a</Brief_Description>
<BiopanningDataSet_Comments>Sixteen clones which inhibited the replication of GCHV in a grass carp kidney cell line were selected. The TCID 50 of GCHV was decreased over 10 000×. Six clones having the strongest inhibitory effect shared the same DNA sequence, with a deduced amino acid sequence of NH(2)-Leu-Trp-Val-Gly-Gly-Gly-Arg-Asn-Ala-COOH.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1747</BiopanningDataSetID>
<Peptides>CTLTTKLYC
CQLGGPSHC
CQKGGPSHC
CQHEMPSKC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:12021868</Reference>
<Target_Name>Newcastle disease virus, NDV</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>A fusion phage carrying the amino acid sequence TLTTKLY was selected from the panning procedure. An antibody competition assay showed that the selected phage was capable of competing with the polyclonal antibodies raised against NDV for binding sites on the virus. Determination of the binding affinity of this phage with NDV by an equilibrium binding assay in solution revealed two different dissociation constants, suggesting that there could be two distinct binding sites for the phage on NDV. Synthetic peptides with the sequence CTLTTKLYC, either in linear or cyclic conformations inhibited the binding of phage bearing the same sequence to NDV.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1748</BiopanningDataSetID>
<Peptides>CTLTTKLYC
CTLTTKAYC
CTLTTPELC
CTPTPRLYC
CTPSPRLYC
CTVWTSEHC
CQLGGPSHC
CQKGGPSDC
CQKGGPSHC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:12021868</Reference>
<Target_Name>Newcastle disease virus, NDV</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>A fusion phage carrying the amino acid sequence TLTTKLY was selected from the panning procedure. An antibody competition assay showed that the selected phage was capable of competing with the polyclonal antibodies raised against NDV for binding sites on the virus. Determination of the binding affinity of this phage with NDV by an equilibrium binding assay in solution revealed two different dissociation constants, suggesting that there could be two distinct binding sites for the phage on NDV. Synthetic peptides with the sequence CTLTTKLYC, either in linear or cyclic conformations inhibited the binding of phage bearing the same sequence to NDV.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1749</BiopanningDataSetID>
<Peptides>CTLTTKLYC
CNLTTKLYC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12021868</Reference>
<Target_Name>Newcastle disease virus, NDV</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>Thirty-nine out of 40 phages analyzed from the third round carried the sequence TLTTKLY and only one related sequence was identified in which its first residue, Thr (T), was substituted by Asn (N). An antibody competition assay showed that the selected phage was capable of competing with the polyclonal antibodies raised against NDV for binding sites on the virus. Determination of the binding affinity of this phage with NDV by an equilibrium binding assay in solution revealed two different dissociation constants, suggesting that there could be two distinct binding sites for the phage on NDV. Synthetic peptides with the sequence CTLTTKLYC, either in linear or cyclic conformations inhibited the binding of phage bearing the same sequence to NDV.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1750</BiopanningDataSetID>
<Peptides>CHPQFEALC</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:12021868</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5,</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>Biopanning gave a consensus sequence of HPQFEAL, which was about 70% of the total phages screened from the third round of panning.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>