<result><BiopanningDataSet><Item><BiopanningDataSetID>1976</BiopanningDataSetID>
<Peptides>AAIMHQEQESNT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:22720103</Reference>
<Target_Name>Anti-VSG LiTat 1.5 polyclonal antibody</Target_Name>
<Template_Name>Variant surface glycoproteins LiTat 1.5, VSG LiTat 1.5</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 negative selection was conducted with endemic negative serum antibodies coated on magnetic particles.</Brief_Description>
<BiopanningDataSet_Comments>One of 188 phage clones reacted in the sandwich ELISA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1977</BiopanningDataSetID>
<Peptides>SAGFENDGTKLA(1)
TGLPTTNKQTSS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:22720103</Reference>
<Target_Name>Anti-VSG LiTat 1.5 polyclonal antibody</Target_Name>
<Template_Name>Variant surface glycoproteins LiTat 1.5, VSG LiTat 1.5</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 negative selection was conducted with endemic negative serum antibodies coated on magnetic particles.</Brief_Description>
<BiopanningDataSet_Comments>Two of 188 phage clones reacted in the sandwich ELISA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1978</BiopanningDataSetID>
<Peptides>AYSKPTIKLANP(3)
LPLATADKNGRT(1)
DKLDNPGGPTVG(2)
LQMPHNSKTANP(1)
INGQFSLKYRNP(1)
LMPNKISNFASA(1)
DQTCNSPPCPPL(1)
STLPPPQGKIIH(1)
WYPLHSGLRSYY(1)
NKSTTNDFLRSP(1)
NGDYLQYKAPNP(1)
NTVRPPTLFYHW(1)
WHSEYQEPYPLS(1)
LDKNVLSPPMPL(1)
HHMSWYSRWLPV(1)
WWKPWSNFYGST(1)
LNTQNHAPLPSI(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>17</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22720103</Reference>
<Target_Name>Anti-VSG LiTat 1.5 polyclonal antibody</Target_Name>
<Template_Name>Variant surface glycoproteins LiTat 1.5, VSG LiTat 1.5</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 negative selection was conducted with endemic negative serum antibodies coated on magnetic particles.</Brief_Description>
<BiopanningDataSet_Comments>Seventeen of 188 phage clones reacted in the sandwich ELISA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1979</BiopanningDataSetID>
<Peptides>QWGWNMPLVEAQ
LLADTTHHRPWT
HSHLHIHSGIQA
NHVHRMHATPAY
HSSHHQPKGTNP
HSSPHFSRTWAS
HYQHNTHHPSRW
HHRTLSPSVSIL
HSSPHFSRHGLL
HHGHSPTSPQVR
NTIHHRHHMPPP
SHNHPPRHTAHS
SSGLRHSHHQHP
HSKLNNRHHALL
HTKPHHTPTQRA
GHIHSMRHHRPT</Peptides>
<Motif>HS-X(2)-H</Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22720657</Reference>
<Target_Name>Oxygen-terminated sides of single-crystalline ZnO (000-1)</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></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1980</BiopanningDataSetID>
<Peptides>ERSWTLDSALSM
SNNDLSPLQTSH
DSSNPIFWRPSS
SILSTMSPHGAT
SHALPLTWSTAA
LLADTTHHRPWT
HVSIHRTTHHEM
MKPDKAIRLDLL
HYPTAKFHAERL
TKNMLSLPVGPG
FNTGSQMHQKFP
HSSHHQPKGTNP
HHTHRVDVHQTR
FGLTAPRSASIL
APRLPQSLLPQL
HHGHSPTSPQVR
SHNHPPRHTAHS
HSKLNNRHHALL
HTKPHHTPTQRA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22720657</Reference>
<Target_Name>Zinc-terminated sides of single-crystalline ZnO (0001)</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>1981</BiopanningDataSetID>
<Peptides>RRRKRPIRRKLR(1)
HIRLTLSRNKNT(1)
TRTMTMNQNRRS(1)
PQTNQTTMKMRM(1)
IMPTKKIPPIIM(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:22743126</Reference>
<Target_Name>Helicase, Hel</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>1982</BiopanningDataSetID>
<Peptides>KKTPPIRIRHRP(1)
NIPIKPRPRLMK(1)
SPHIIRNHRLSK(1)
HRILMRIRQMMT(1)
RIIRKSQRSLMN(1)
RQPRTPMTRLSR(1)
IIRHRSMIITIT(1)
KTRTMQMRNRMP(1)
RMRSKRRKITTR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22743126</Reference>
<Target_Name>RNA-directed RNA polymerase, Pol, RdRp</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>P9 (HRILMRIRQMMT) exerted the highest antiviral activity with an IC50 of 56 mM, and the minimum toxicity to cells. It was proved that p9 inhibited PRRSV replication in infected MARC-145 cells in a dose-dependent manner, and the amino acid sequence of HRILMRIR was important for antiviral activity of p9. Also, p9 could bind to the cell membrane and penetrated into cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1983</BiopanningDataSetID>
<Peptides>AGKGTPSLETTP(4)
GPLPKTYAIPSS(2)
AHQANFPSSSAI(1)
DNVHTTLSQPST(1)
FPSSSNHYPWAE(1)
KLTTNPSSPLNY(1)
TPRAELHFGQSS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20145035</Reference>
<Target_Name>Hepatocellular carcinoma cell lines BEL-7402</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>Phage binding assay was performed by using cell-based ELISA. The absorbance at 450 nm was determined. Selectivity is calculated using the following formula: Selectivity = (ODS1-ODC1)/(ODS2-ODC2). Here, ODS1 and ODC1 represent the values of the binding to BEL-7402 cells by the selected phage and control phage, respectively; ODS2 and ODC2 represent the values of the binding to control cell line HL-7702 by the selected phage and control phage, respectively. The phages with selectivity above 2 are considered to be positive clones. Phage clones A54, A67, and B2 seemed to have the most specific binding ability in cell-based ELISA. It was found that the peptide sequences AGKGTPSLETTP, TPRAELHFGQSS and AHQANFPSSSAI were displayed on phage clone A54, B2 and A67, respectively.</Affinity_Measurement_Description>
<Brief_Description>Tumor was raised by s.c. injection of 1.0e6 BEL-7402 cells per mouse in 200μL culture medium with 10% FCS into the flanks of the nude mice. When tumors reached a size of ∼1 cubic centimeter, phage library containing e11 colony-forming units (CFU) was injected through the tail veins of the mouse.</Brief_Description>
<BiopanningDataSet_Comments>After phage A54 (AGKGTPSLETTP) was injected i.v. into the xenograft-bearing mice for in vivo distribution, phage enrichment was found in tumor tissues compared with control phage C10 and normal liver tissues through phage titering and immunohistochemical staining. Next, the specific binding ability of synthesized peptide A54 was further confirmed by fluorescence microscopy, competition binding, and fluorescence-activated cell sorting assay. A54 and A54M (sequence AGKGTAALETTP) were synthesized and coupled to doxorubicin (DOX) to do the preliminary targeting therapy. After the treatment, the proliferation of liver cancer cells treated with A54-DOX was restrained significantly in vitro when compared with A54M-DOX-treated group. Reduction in tumor size and prolongation of long-term survival were also found in xenograft-bearing models compared with free DOX-treated group. In conclusion, the specific binding peptide A54, which was screened from phage display library, represents a promising approach for the development of novel target therapy strategies against hepatocellular carcinoma.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1984</BiopanningDataSetID>
<Peptides>WMPSDVDINDPQ
QPKPAAEAASKK
WYSSMSEDKRGW</Peptides>
<Motif></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:22123020</Reference>
<Target_Name>Zirconia</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>DNA sequencing of the corresponding portion of Ф#17 (WMPSDVDINDPQGGGSRPNLHQPKPAAEAASKKKSENRKVPFYSHSWYSSMSEDKRGW) unexpectedly revealed that it displayed a 58-mer peptide. The authors found that Ф#17 had a 300-fold, significantly higher binding affinity for zirconia discs than phages displaying no peptide. In quartz crystal microbalance assay, a rapid increase in energy dissipation was observed from Ф#17 but not from the control phages, indicating that Ф#17 binds to the surface of zirconia via its displayed peptide.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1985</BiopanningDataSetID>
<Peptides>YITPYAHLRGGN(14)</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:22435500</Reference>
<Target_Name>Amorphous spherical silica particles (15 nm diameter)</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>1986</BiopanningDataSetID>
<Peptides>KSLSRHDHIHHH(20)</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:22435500</Reference>
<Target_Name>Amorphous spherical silica particles (82 nm diameter)</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>1987</BiopanningDataSetID>
<Peptides>LDHSLHS(16)</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:22435500</Reference>
<Target_Name>Amorphous spherical silica particles (82 nm diameter)</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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1988</BiopanningDataSetID>
<Peptides>MHRSDLMSAAVR(20)</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:22435500</Reference>
<Target_Name>Amorphous spherical silica particles (450 nm diameter)</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>1989</BiopanningDataSetID>
<Peptides>NSWTNASLSTFH
NSRTNNSQWTFQ
ESWTNSWAHYFG
ESWTNSWAMYFG
QSYTNDDVLRIS
QNMNNWTLASIM
EVMNNWTLASIM
ASISNLTLSRFM
HSWSNYWGHQHA
HRISNYAMELHS
HSLTNTQMTQLS
HSLSNIQMATLA
HRMTNAMHHFMG
HRMTNNAMDVFM
HRLTNSEQAALP
TAVTNSMMERLW
GWGNKTPSQDVH
DYTNSVSMRYLS
HQLSNKDEQTPQ
ADPFSPTNRIPL</Peptides>
<Motif>HSWTNSWMATFL</Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22508944</Reference>
<Target_Name>Anti-MDA-LDL monoclonal antibody LR04</Target_Name>
<Template_Name>Malondialdehyde-modified LDL (MDA-LDL)</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>Control IgM was used in the negative selection, and then unbound phages were transferred to wells coated with LRO4 (positive selection). In the last biopanning round, LRO4-bound phages were competitively eluted with increasing concentrations (3-150 μg/ml) of MDA-LDL diluted in blocking buffer, followed by elution using elution buffer.</Brief_Description>
<BiopanningDataSet_Comments>Dodecamer peptide sequences were aligned by the Clustal W program to obtain consensus sequences, a dodecamer linear peptide P1 (HSWTNSWMATFL).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1990</BiopanningDataSetID>
<Peptides>CNNWNMPLC
CNNRNMPLC
CNNYNMPLC
CNNQNMPLC
CNNWKMPLC
CNNSHMPLC
CKNSXQPLC
CNNSXMPLC
CQNSHMPLC
CNNSNMPLC
CNNSKMRLC
CDWAPHFTC </Peptides>
<Motif>CNNSNMPLC</Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22508944</Reference>
<Target_Name>Anti-MDA-LDL monoclonal antibody LR04</Target_Name>
<Template_Name>Malondialdehyde-modified LDL (MDA-LDL)</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>Control IgM was used in the negative selection, and then unbound phages were transferred to wells coated with LRO4 (positive selection). In the last biopanning round, LRO4-bound phages were competitively eluted with increasing concentrations (3-150 μg/ml) of MDA-LDL diluted in blocking buffer, followed by elution using elution buffer.</Brief_Description>
<BiopanningDataSet_Comments>Heptamer peptide sequences were aligned by the Clustal W program to obtain consensus sequences, a cysteine-constrained heptamer cyclic peptide P2(CNNSNMPLC).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1991</BiopanningDataSetID>
<Peptides>CTSYNEPLC
CNLYNEPLC
CNLYNEPFC
CTVFNEPFC</Peptides>
<Motif>C-x(2)-[YF]-N-E-P-[LF]-C</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:23006741</Reference>
<Target_Name>Anti-VACV A33  monoclonal antidbody</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>MAb-1G10 binding peptides were isolated from the conformational library screening, none of which contain vaccinia virus A33 sequence.One consensus motifs were identified:C-x(2)-[YF]-N-E-P-[LF]-C.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1992</BiopanningDataSetID>
<Peptides>CQLKWPFEC
CKPTWPFEC
CSNSWPHEC
CCDDWPHEC
CQTSYPYEC
CWYDSLIFC</Peptides>
<Motif>C-x(3)-W-P-[FH]-E-C</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:23006741</Reference>
<Target_Name>Anti-VACV A33  monoclonal antidbody</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>MAb-1G10 binding peptides
were isolated from the conformational library scree-ning, none of which contain vaccinia virus A33 sequence. One consensus motifs were identified: C-x(3)-W-P-[FH]-E-C. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1993</BiopanningDataSetID>
<Peptides>MKPALCEPLCGM(5)
NPYCEPVCQDWA(1)
SLMRELCEPRCE(1)
QLTAQHRDSLSS(1)</Peptides>
<Motif>C-E-P-L-C</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:23006741</Reference>
<Target_Name>Anti-VACV A33  monoclonal antidbody</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 conformationally constrained CEPLC sequence was likely to be functionally identical to the minimal core MAb-1G10
epitope.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1994</BiopanningDataSetID>
<Peptides>CNSHNHHTC[0.055]
CHHNLTHAC[0.248]
CLKQLQRGC[0.143]
CLHHYHGSC[0.330]
CTLYHNAGC[NG]</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:22759068</Reference>
<Target_Name>Protein tyrosine phosphatases(PTPRJ-His6)</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>In phage ELISA, ELISA absorbance values of single phage clones were expressed as the difference between OD405 nm and OD629 nm. NG denotes not given.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1995</BiopanningDataSetID>
<Peptides>WPPKAMTQLGIKAC
CGHGLKVQSTLGAC
CKPYPKVYGLTGMC
CQKLAWLTGKKEKC
CTSKPQRWFGLPC
CPPKLEQWYDGC</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:11179221</Reference>
<Target_Name>G protein β1γ1 subunits</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>f88-4 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1996</BiopanningDataSetID>
<Peptides>CEKRYGIEFC
CEKRLGVRSC</Peptides>
<Motif>E-K-R-x-G-x(3)</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:11179221</Reference>
<Target_Name>G protein β1γ1 subunits</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>f88-4 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1997</BiopanningDataSetID>
<Peptides>YPWLQSY(6)
LSTTLPL(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22828501</Reference>
<Target_Name>Lens epithelium-derived growth factor (LEDGF)/p75</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>We first depleted the M13-derived linear 7-mer peptide phage librariy by preabsorbing the library on beads coated with wild-type HIV-1 IN.Phages remaining in the supernatant were used for positive selection rounds with  LEDGF-coated beads .</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1998</BiopanningDataSetID>
<Peptides>CVMGHPLWC(4)
CILGHSDWC(3)
CVSGHPLWC(2)
CVEGHPAWC(1)
CVSGHPEFC(1)
CVMGHPTWC(1)
CVMGHPSWC(1)</Peptides>
<Motif>V-x-G-H-P-x-W</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22828501</Reference>
<Target_Name>Lens epithelium-derived growth factor (LEDGF)/p75</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>We first depleted the M13-derived cyclic 7-mer peptide phage librariy by preabsorbing the library on beads coated with wild-type HIV-1 IN. Phages remaining in the supernatant were used for positive selection rounds with  LEDGF-coated beads.</Brief_Description>
<BiopanningDataSet_Comments>Several of the isolated cyclic peptides(CPs) have a common motif (VM/xGHPL/xW) without linear or conformational homology to IN.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1999</BiopanningDataSetID>
<Peptides>FPWMQSYGVGIN(30)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22828501</Reference>
<Target_Name>Lens epithelium-derived growth factor (LEDGF)/p75</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>We first depleted the M13-derived 12-mer peptide phage librariy by preabsorbing the library on beads coated with wild-type HIV-1 IN. Phages remaining in the supernatant were used for positive selection rounds with  LEDGF-coated beads.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2000</BiopanningDataSetID>
<Peptides>IPLPPPSRPFFK</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:22791264</Reference>
<Target_Name>Platelet-derived growth factor receptor β (PDGFRβ)</Target_Name>
<Template_Name>Platelet-derived growth factor subunit B</Template_Name>
<Structure_of_Target_Template_Complex>3MJG,</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>e11 plaque-forming units were added on immobilized negative target (EGFR) in 96-well plates. After incubation for 1 h at room temperature, medium containing unbound phages was transferred on the immobilized positive target (PDGFRβ) and further incubated for 1 h at room temperature.</Brief_Description>
<BiopanningDataSet_Comments>40% of the clones isolated on immobilized protein displayed the peptide sequence: IPLPPPSRPFFK.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>