<result><BiopanningDataSet><Item><BiopanningDataSetID>1501</BiopanningDataSetID>
<Peptides>DLCLRDWGCLW[+++]</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:12119302</Reference>
<Target_Name>Rat serum albumin</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 and  X(2)CX(j)CX(2) M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, the absorbance at 405 nm was monitored.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1502</BiopanningDataSetID>
<Peptides>DTCVDLVRLGLECWG[+++]</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:12119302</Reference>
<Target_Name>Rat serum albumin</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>X(2)CX(j)CX(2) M13 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, the absorbance at 405 nm was monitored.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1503</BiopanningDataSetID>
<Peptides>MSRNFSGTTPRHLLL(2)
SVHQLNAPRSLLFNH(1)
LPPRNLLYGNSRLDW(1)
YRPISNMPRQLLMRL(1)
MDTPRHLMAYLITQR(2)
LMNSPRQLMTRKMSH(1)
TIPSAKSPRSLFVTH(1)
STSPPRSLLGSLDRT(1)
LTHHPHYPRHLMGSR(1)
LPPSEASTPRRLLHQ(1)
PRSLLSPSDSLRFIT(1)
PRNLFLPTAHPFST(1)
TEFITREARHLLLIP(1)
FQEPKSEQRHLFYKW(2)</Peptides>
<Motif>P-R-H-L(2)</Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:7507752</Reference>
<Target_Name>Anti-ATPase alpha-1 subunit monoclonal antibody M8-P1-A3</Target_Name>
<Template_Name>Sodium/potassium-transporting ATPase subunit alpha-1</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X15 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The M8-Pl-A3 epitope was found to consist of the five amino acid 494-PRHLL-498 sequence stretch of α, with residues PRxLx being critical for antibody recognition.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1504</BiopanningDataSetID>
<Peptides>KFYRFL(7)
DRFRHI(2)
KFDRFL(1)
KLYRFL(1)
KLYGFV(1)
DRFRQV(1)
EFDRFR(1)
QKPIKL(1)
DLLRGA(1)
NMPKPI(1)</Peptides>
<Motif>KFDRFL, DRFR</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:8956081</Reference>
<Target_Name>Anti-sperm whale myoglobin polyclonal antibody</Target_Name>
<Template_Name>Myoglobin</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>Phages displaying a ligand for the biotinylated polyclonal antibodies are captured on the dish by binding of the biotin moiety to immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments>Motif KFDRFL, which matches amino acid residues 42-47 the sperm-whale myoglobin sequence.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1505</BiopanningDataSetID>
<Peptides>RFDRLK(8)
LELFRR(4)
RFDWLK(1)
GFDRLK(1)
LELFRG(1)
LGLFRR(1)
RCDRLM(1)
RVDRLM(1)
LEVCSE(1)
GCDLYI(1)</Peptides>
<Motif>RFDRLK, LELFRR, DRLM</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:8956081</Reference>
<Target_Name>Anti-sperm whale myoglobin polyclonal antibody</Target_Name>
<Template_Name>Myoglobin</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>Phages displaying a ligand for the biotinylated polyclonal antibodies are captured on the dish by binding of the biotin moiety to immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments>Two motifs show homology to the sperm-whale myoglobin sequence: RFDRLK, which matches amino acid residues 45-50 (RFKHLK), and LELFRR, which matches amino acid residues 135-140 (LELFRK).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1506</BiopanningDataSetID>
<Peptides>YWYRWS(5)
HWYRFM(3)
QRYRFH(2)
WLYRFS(2)
QLYRFH(1)
YFYRFR(1)
KFYRFL(1)
QWYRFM(1)
FWNRFA(1)
KWNRFA(1)
HWNRFV(1)
VWWRFM(1)
YLYRPY(1)</Peptides>
<Motif>HWYRFM, QRYRFH, YWYRWS,YRF, WNRF</Motif>
<Unique_Sequence_Number>13</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:8956081</Reference>
<Target_Name>Anti-sperm whale myoglobin polyclonal antibody</Target_Name>
<Template_Name>Myoglobin</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>Phages displaying a ligand for the biotinylated polyclonal antibodies are captured on the dish by binding of the biotin moiety to immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1507</BiopanningDataSetID>
<Peptides>REDLFDRYAHLRTPV
QTNVKYDRFDWLLRQ
KYDRFVIYKDGSVQT
ELREEYKQLGYTGPH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:8956081</Reference>
<Target_Name>Anti-sperm whale myoglobin polyclonal antibody</Target_Name>
<Template_Name>Myoglobin</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>X15 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Phages displaying a ligand for the biotinylated polyclonal antibodies are captured on the dish by binding of the biotin moiety to immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-six samples were sequenced after two rounds of screening. It was found that except for 19% (5/26) of the positive clones containing the insert sequence of D-R-F, there were a few dominant sequence motifs. However, with the help of the Blitz electronic mail server, four sequences were found to show homologies to the myoglobin sequence. Three of the insert peptide sequences (clones REDLFDRYAHLRTPV, QTNVKYDRFDWLLRQ and KYDRFVIYKDGSVQT) showed similarities to amino acid residues 42-50 of the myoglobin sequence, On the other hand, the peptide insert sequence of clone ELREEYKQLGYTGPH was similar to amino acid residues 141-153 of the myoglobin sequence (which was located in the C-terminus of the protein).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1508</BiopanningDataSetID>
<Peptides>RLAPEPDDPITPMTK(2)[1.25 ± 0.06, 22 ± 3%]
KLLPEDDESRTYHTV(1)[1.32, 19%]
TQSYPPPPAWRAASR(1)[2.11, 53%]
QLSPESDYDDHGMRY(1)[3.00, 40%]
KLFPEEDEMRTETQR(1)[1.60, 24%]
SQSYPEPARGSVPMP(1)[3.00, 29%]</Peptides>
<Motif>L-x-P-E-x-D, QSYP, E-x-[ED]-P(2)-V</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:12501244</Reference>
<Target_Name>Anti-TPO monoclomal antibody T13</Target_Name>
<Template_Name>Thyroid peroxidase, TPO</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>X15 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 490 nm corresponding to the binding of each clone to aAb T13 was shown. The binding of each clone to aAb T13 was inhibited by soluble human TPO at 90 nM; only clones showing an inhibition greater than 15% with hTPO are indicated. When a clone was represented at least twice, the absorbance and percent inhibition values are given as the mean value ± S.D.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Mimotope sequence alignment on the TPO molecule, together with the binding analysis of the T13 aAb on TPO mutants expressed by Chinese hamster ovary cells, demonstrated that regions 353-363, 377-386, and 713-720 from the myeloperoxidase-like domain and region 766-775 from the complement control protein-like domain are a part of the IDR recognized by the recombinant aAb T13. Furthermore, authors demonstrated that these regions were involved in the binding to TPO of sera containing TPO-specific autoantibodies from patients suffering from Hashimoto\'s and Graves\' autoimmune diseases.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1509</BiopanningDataSetID>
<Peptides>GQSYPPRPDTSLHVT(1)[0.50, 28%]
ELNPEPDTEVFPMTF(1)[0.91, 38%]
KNSRQSYPEPAPVYH(1)[0.59, 28%]
ENEPPVWTTESKLQS(1)[0.74, 31%]
ESDPPVASYQWRLIN(1)[0.79, 36%]
ESVMQSYPPHLQIPG(1)[0.50, 24%]</Peptides>
<Motif>L-x-P-E-x-D, QSYP, E-x-[ED]-P(2)-V</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:12501244</Reference>
<Target_Name>Anti-TPO monoclomal antibody T13</Target_Name>
<Template_Name>Thyroid peroxidase, TPO</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>X15 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 490 nm corresponding to the binding of each clone to aAb T13 was shown. The binding of each clone to aAb T13 was inhibited by soluble human TPO at 90 nM; only clones showing an inhibition greater than 15% with hTPO are indicated. When a clone was represented at least twice, the absorbance and percent inhibition values are given as the mean value ± S.D.</Affinity_Measurement_Description>
<Brief_Description>Bound phages were eluted by competition with a TPO solution.</Brief_Description>
<BiopanningDataSet_Comments>Mimotope sequence alignment on the TPO molecule, together with the binding analysis of the T13 aAb on TPO mutants expressed by Chinese hamster ovary cells, demonstrated that regions 353-363, 377-386, and 713-720 from the myeloperoxidase-like domain and region 766-775 from the complement control protein-like domain are a part of the IDR recognized by the recombinant aAb T13. Furthermore, authors demonstrated that these regions were involved in the binding to TPO of sera containing TPO-specific autoantibodies from patients suffering from Hashimoto\'s and Graves\' autoimmune diseases.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1510</BiopanningDataSetID>
<Peptides>FSLSKPP(21)[0.468 ± 0.011]
STQAMFQ(9)[0.523 ± 0.047]
HSMQLST(4)[0.436 ± 0.047]
HAIYPRH(3)[0.782 ± 0.022]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12951773</Reference>
<Target_Name>A549 bronchial epithelial cell line</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, absorbance at 420 nm was measured. Data shown were reproduced from the bar graph and expressed as means ± standard deviations. The absorbance of the negative control phage was 0.379 ± 0.024. Results demonstrated the isolated phage displaying HAIYPRH, STQAMFQ, and FSLSKPP show significantly increased levels of binding to A549 cells compared with a control wild-type phage displaying no peptide on its surface coat. </Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1511</BiopanningDataSetID>
<Peptides>NVESQPGGQPNT
QYTDHHSSLLGP
LYRPSDSSLAGP
MNVTLSSSLDGP
NGNRSPTTLMGP
DRLLTTLSGPAQ</Peptides>
<Motif>Y-x(4)-S(2)-x(2)-G-P, S(2)-x(2)-G-P, T(2)-x(2)-G-P</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:14629623</Reference>
<Target_Name>Anti-p34 polyclonal antibody</Target_Name>
<Template_Name>34 kDa antigenic protein</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>Immunization of mice with these peptides elicited an anti-p34 antibody response. Two B-cell epitopes were identified and characterized. Based on the reactivity and the type of immune response elicited, epitope A was determined to be conformational, whereas epitope B was demonstrated to be sequential. Both epitopes were shown to be present in p34 proteins from M. avium ssp. avium or M. paratuberculosis but absent from M. intracellulare, the other member of the M. avium complex. Furthermore, both epitopes were mapped to regions of p34 that display high variability when compared to homologous proteins from other mycobacterial species of public and animal health importance.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1512</BiopanningDataSetID>
<Peptides>SHSALTVPLYHA
WSDMSMYSHLMP
MSDSHYNSQSSV</Peptides>
<Motif>SH</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:11932389</Reference>
<Target_Name>Anti-PRRSV neutralizing monoclonal antibody ISU25-C1</Target_Name>
<Template_Name>Sequential epitope on GP5</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The resin was washed with TBS containing 0.05% Tween 20 in the first panning, TBS containing 0.1% Tween 20 in the second panning, and TBS containing 0.5% Tween 20 in the third panning. Phages bound to ISU25-C1 were eluted with 100 mM glycine, pH 2.5.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1513</BiopanningDataSetID>
<Peptides>SHITSYHPAYFW[0.500 ± 0.003]</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:11932389</Reference>
<Target_Name>Anti-PRRSV neutralizing monoclonal antibody ISU25-C1</Target_Name>
<Template_Name>Sequential epitope on GP5</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>Results of phage ELISA are shown above and expressed as corrected OD at 405 nm (OD for selected phage - OD for unselected phage library) ± standard deviation.</Affinity_Measurement_Description>
<Brief_Description>In the second panning, a CNBr-activated Sepharose-coupled MAb was used. In the third panning, protein G was used again to capture the phage-antibody complexes from solution. The resin was thoroughly washed with 10 mM Tris, pH 7.5, in the first panning, with 10 mM Tris, pH 7.5, containing 0.5 M NaCl in the second panning, and with 10 mM Tris, pH 7.5, containing 0.05% Tween 20 in the third panning.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1514</BiopanningDataSetID>
<Peptides>ALVNIPISNNLA[0.045 ± 0.008]
ALVNWHGVYNYR[NT]
ALVNNSHTMPLW[NT]
ALVNSPLTRAPM[NT]
GGYPQQMVRHFA[NT]
KIPYNLSFMVPP[NT]</Peptides>
<Motif>ALVN</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:11932389</Reference>
<Target_Name>Anti-PRRSV polycolonal antibody</Target_Name>
<Template_Name>Prcine reproductive and respiratory syndrome virus, RSV</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>Results of phage ELISA  are shown and expressed as corrected OD at 405 nm (OD for selected phage - OD for unselected phage library) ± standard deviation. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Anti-PRRSV affinity-purified antibodies with high SN titer were used to select phages from the library, and several clones carrying amino-terminal motif ALVN were recovered. This is a consensus motif found in residues 27 to 30 of PRRSV GP5. Another clone (KIPYNLSFMVPP) selected with the swine antibodies with high SN titer expressed a peptide with a YNL motif, which is also a consensus motif found in amino acids 43 to 45 of PRRSV GP5. Finally, clone KIPYNLSFMVPP carried an HF motif, which is found in residues 38 to 39 of GP5 of a PRRSV IA 97-7895 isolate, which was the primary PRRSV strain used to immunize the pigs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1515</BiopanningDataSetID>
<Peptides>YKNTHLDLIYNA[0.080 ± 0.001]
NSAVHFQRQFSQ[NT]</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:11932389</Reference>
<Target_Name>Anti-peptide SGSGANNSSSSHFQSIYNC polyclonal antibody</Target_Name>
<Template_Name>Prcine reproductive and respiratory syndrome virus, RSV</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>Results of phage ELISA are shown and expressed as corrected OD at 405 nm (OD for selected phage - OD for unselected phage library) ± standard deviation. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Anti-peptide S2 affinity-purified antibodies were used to select phages from the library, and 4 out of 12 selected clones corresponded to a single clone (YKNTHLDLIYNA), containing an HLXLIYN motif. This motif is also found between amino acids 38 and 44 of the consensus sequence of PRRSV GP5. Another clone selected with these antibodies (NSAVHFQRQFSQ) contained an HFQ motif located between residues 38 and 40 of GP5 of the PRRSV Iowa strain.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1516</BiopanningDataSetID>
<Peptides>APWHLSSQYSRT(11)[0.932 ± 0.046]
HGEVPRFHAVHL(6)[0.952 ± 0.089]
HPVTRFHNPVEY(2)[0.744 ± 0.026]
LISSATPFSPNK(1)[0.606 ± 0.089]
WSSGMTPDTGAP(1)[0.661 ± 0.020]</Peptides>
<Motif>V-[PT]-R-F-H-[AP]-V, [MA]-T-P</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:20508256</Reference>
<Target_Name>Rhesus monkey neural stem cells (R-NS cells)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, the absorbance at 492 nm was determined. Data were reproduced from the graph and shown as means ± standard derivations. The absorbance of M13 wild-type phage (Wt) as negative control was 0.019. Besides, results of a competitve assay showed that the synthetic HGE peptide (HGEVPRFHAVHL) could compete with the HGE phage, achieving 50% inhibition at the concentration of about 500 nM. Further results of Western blot showed that the HGE peptide interacted with 48/34-kDa proteins on the membrane of neural stem cells.</Affinity_Measurement_Description>
<Brief_Description>The periphery cells and rhesus monkey ES cells were used as a negative selection.</Brief_Description>
<BiopanningDataSet_Comments>Combined with quantum dots, the HGEVPRFHAVHL peptide can be used as a direct tool to show optical imaging of specific binding on a single cell membrane. Further results of Western blot showed that the HGEVPRFHAVHL peptide interacted with 48/34-kDa proteins on the membrane of neural stem cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1517</BiopanningDataSetID>
<Peptides>AETVESCLAKSH(9)
ALTLHPQPLDHP(4)
QNMMSPIEGVRI(1)
APRYTQTPQALA(1)
FMGPQESTLQRL(1)
TALATSSTYDPH(1)
KSWLPLSQEVRF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:20350526</Reference>
<Target_Name>Bacillus cereus ATCC 4342</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 method enabled us to identify two 12-amino acid consensus peptide sequences (AETVESCLAKSH and ALTLHPQPLDHP) that specifically bind to B. cereus 4342 and B. anthracis Sterne, the nonpathogenic surrogates of B. anthracis strain.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1518</BiopanningDataSetID>
<Peptides>DSLQASAT[100, 17]
ADLTVQAN[97, 2]
AELTTRAE[94, 3]
DQLNATAL[113, 1]
DQLTVSAQ[84, 18]
DSLHGQAM[157, 1]
DSLTLQAQ[79, 3]
DTLTHEAT[63, 2]
EDLTQRAL[66, 3]
SNLEMMAT[100, 1]
DDLTASAI[1, 130]
DELITEAH[&lt;1, 160]
DELTVAAN[0, 142]
DLLTTQAE[&lt;1, 94]
DNLEMMAQ[1, 104]
DNLITMAD[&lt;1, 105]
DSLNEQAV[1, 138]
DTLTENAV[0, 160]
EDLNAQAL[1, 113]
EDLSAMAG[1, 115]
EELESIAN[&lt;1, 129]
EELNGQAM[1, 130]
EELNQQAN[1, 104]
EELSNSAT[2, 123]
EELSQQAN[1, 153]
EELSVQAT[1, 107]
EELTLEAH[1, 146]
EELTNSAQ[&lt;1, 168]
ELLEAQAK[2, 94]
ELLTDQAS[&lt;1, 122]
ENLNEVAM[1, 130]
EQLENQAI[2, 123]
EQLEVQAS[1, 120]
EQLSSEAN[1, 179]
EQLSSNAE[0, 132]
EQLTVEAS[2, 113]
ESLAAEAT[1, 152]
ESLEAQAT[1, 137]
ESLTENAY[&lt;1, 133]
ETLENMAS[&lt;1, 97]
ETLEQQAT[1, 114]
ETLEVQAQ[2, 111]
ETLTESAA[1, 148]
LDLHEAAV[&lt;1, 135]
QELSIQAE[1, 119]
SLLSNQAE[1, 131]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>46</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19633313</Reference>
<Target_Name>β-galactosidase</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>G-α phage display library (XXLXXXAX)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>ELISA signals are normalized against the 1G40 phage (displaying DSLQASAT) ELISA signal in direct ELISA. ELISA signals are normalized against the signal of the sample without phage in competitive ELISA. Both normalized ELISA signals were shown. Normalized ELISA signals of control phage in the direct format and in the competition format were &lt;1 and 115, respectively.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1519</BiopanningDataSetID>
<Peptides>AYLADRAD(34)
FDLQLLAE(4)
AYLLLRAD(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:12538914</Reference>
<Target_Name>Bovine fibrinogen</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>f8 α phage display library (XXLXXXAX)</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>1520</BiopanningDataSetID>
<Peptides>EAGPRAAP(3)
EAGPRSTP(3)
EAGPRSSP(2)
EAGPRSAP(1)
EAGPRSNP(1)
AAGPRPTS(1)
EAGPRSTQ(1)
VAGPREVP(1)
VAGPRMTE(1)
VAGPREVS(1)
EAGPRASP(1)
AGPREPNL(1)
EAGPRSQP(1)
EGYLRPDT(1)
DGFLRPE(1)
EGYLRPES(1)
EGYMRPDP(1)
DGFLRPDP(1)
DGFLRPDS(1)
EGFTRPSP(1)
DSSVRFTG(1)
AGGPRTAP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>22</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12538914</Reference>
<Target_Name>Bovine fibrinogen</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>f8-8mer phage display library (X8)</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>1521</BiopanningDataSetID>
<Peptides>HGHPYQHLLRVL
DMPRTTMSPPPR</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:19342549</Reference>
<Target_Name>Single-walled carbon nanotubes, SWNTs</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>1522</BiopanningDataSetID>
<Peptides>ANPHTTLRNHVL(1)
SPRLTMPPKVPG(1)
HPSLNLPLPRLV(1)
DLNTYPTLSKRE(1)
VSSYPPPQTLLP(1)
TQNSNSTQYGNR(1)
DRPPHLGDPPHM(1)</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>DOI:10.1002/adma.200702322</Reference>
<Target_Name>Hydroxyapatite, HA</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>This step was necessary to remove any phage with strong affinity to the polypropylene filter tube. The library was then used to perform the subsequent selection against hydroxyapatite (HA).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1523</BiopanningDataSetID>
<Peptides>QHTNIVNTQSRV(1)
KLPPINLHPHRL(1)
TAPASMSDDRAS(1)
SILSTMSPHGAT(1)
SSPDRALAATPF(1)
LLADTTHHRPWT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>DOI:10.1002/adma.200702322</Reference>
<Target_Name>Hydroxyapatite, HA</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>This step was necessary to remove any phage with strong affinity to the polypropylene filter tube. The library was then used to perform the subsequent selection against hydroxyapatite (HA).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1524</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(19)
SVSVGMNPSPRP(1)
SAHGTSTGVPWP(1)
FPWLPRDNHTLN(1)
AVSSLSSTNYSI(1)
TMGPTAPRFPHY(1)
QSHTRHISPAQV(1)
SAKTLSNSPLSN(1)
DAQQITLSHWRC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>DOI:10.1002/adma.200702322</Reference>
<Target_Name>Hydroxyapatite, HA</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>This step was necessary to remove any phage with strong affinity to the polypropylene filter tube. The library was then used to perform the subsequent selection against hydroxyapatite (HA).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1525</BiopanningDataSetID>
<Peptides>CGNSNPKSC(12)
CPHNLTKLC(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:15492500</Reference>
<Target_Name>Human gastric cancer cells</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>After four rounds of selection, one phage was obtained with a cyclic 7-mer peptide CGNSNPKSC homing to human gastric adenocarcinoma . There was a 4.6~137.26-fold increase in the number of the selected phage in gastric cancer xenograft in comparision with control organs brain, heart, liver, spleen and kidney. Immunohistochemistry in mouse and human tissue showed that this phage peptide only bind to the endothelial cells of human gastric cancer. This peptide was observed only specific binding to HUVEC not to SGC-7901, Eca-109, LoVo and Hep-G2 by ELISA. The competitive and inhibitory result between the synthetic CGNSNPKSC peptide and the phage displaying the peptide CGNSNPKSC on HUVEC and in vivo was also confirmed its specific binding effect. This peptide may be a possible candidate for targeted drug delivery in antivascular therapy.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>