<result><BiopanningDataSet><Item><BiopanningDataSetID>2776</BiopanningDataSetID>
<Peptides>HFYQITWLPNTFPAR(15)[0.52 ±0.03, 0.45 ± 0.05]
LSTHTKLNKADIQMP(3)[0.81 ± 0.02, 0.63 ± 0.01]
YRWPSTPSASRQATL(1)[0.53 ± 0.06, 0.41 ± 0.01]
GAARHCQPASPATMM(1)[0.55 ± 0.04, 0.42 ± 0.02]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:25081558</Reference>
<Target_Name>Anti-TsCa IgG</Target_Name>
<Template_Name>T. saginata metacestode crude 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>X15 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Affinities of phages to Anti-TsCa IgG were measured by phage competitive ELISA. Data shown were absorbances at 490 nm and reproduced from Fig. 3b. High titer serum was pre-incubated with TsCa (500 μg/mL) and assayed on phage-coated plates. High titer serum directly incubated with phage-coated plates as control and the values of A490 are the first value in square brackets. There was a little reduction in the absorbance compared with that in the assay without the competitor.</Affinity_Measurement_Description>
<Brief_Description>During the first panning, an immunotube (Nunc) was coated overnight with 5 μg/mL of anti-TsCa IgG. In the second panning, 1 μg/mL of anti-TsCa IgG was used for coating, with 0.5 μg/mL in the subsequent pannings. Affinity-selected phagedisplayed peptides were obtained by competition assay after incubation at room temperature for 90 min with TsCa at a concentration 100 times higher than that of bovine IgG.</Brief_Description>
<BiopanningDataSet_Comments>The peptides HFYQITWLPNTFPAR and YRWPSTPSASRQATL shared similarity with highly conserved proteins from the Taeniidae family with known immunogenicity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2777</BiopanningDataSetID>
<Peptides>TCIWQWPDWACK(1)[0.5 ± 0.02, 0.41 ± 0.03]
FCMSTCSGLKCQ(1)[0.36 ± 0.02, 0.31 ± 0.02]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:25081558</Reference>
<Target_Name>Anti-TsCa IgG</Target_Name>
<Template_Name>T. saginata metacestode crude 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>X6PPX(Y/F)X6 phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Affinities of phages to Anti-TsCa IgG were measured by phage competitive ELISA. Data shown were absorbances at 490 nm and reproduced from Fig. 3b. High titer serum was pre-incubated with TsCa (500 μg/mL) and assayed on phage-coated plates. High titer serum directly incubated with phage-coated plates as control and the values of A490 are the first value in square brackets. There was a little reduction in the absorbance compared with that in the assay without the competitor.</Affinity_Measurement_Description>
<Brief_Description>During the first panning, an immunotube (Nunc) was coated overnight with 5 μg/mL of anti-TsCa IgG. In the second panning, 1 μg/mL of anti-TsCa IgG was used for coating, with 0.5 μg/mL in the subsequent pannings. Affinity-selected phagedisplayed peptides were obtained by competition assay after incubation at room temperature for 90 min with TsCa at a concentration 100 times higher than that of bovine IgG.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2778</BiopanningDataSetID>
<Peptides>VHTSIRPRCQPRAITPR(1)[1.11 ± 0.01, 0.92 ± 0.01]
MGIRALPPCQNARQRLS(1)[0.85 ± 0.02, 0.77 ± 0.01]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:25081558</Reference>
<Target_Name>Anti-TsCa IgG</Target_Name>
<Template_Name>T. saginata metacestode crude 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>X8CX8 f88-based phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Affinities of phages to Anti-TsCa IgG were measured by phage competitive ELISA. Data shown were absorbances at 490 nm and reproduced from Fig. 3b. High titer serum was pre-incubated with TsCa (500 μg/mL) and assayed on phage-coated plates. High titer serum directly incubated with phage-coated plates as control and the values of A490 are the first value in square brackets. There was a little reduction in the absorbance compared with that in the assay without the competitor.</Affinity_Measurement_Description>
<Brief_Description>During the first panning, an immunotube (Nunc) was coated overnight with 5 μg/mL of anti-TsCa IgG. In the second panning, 1 μg/mL of anti-TsCa IgG was used for coating, with 0.5 μg/mL in the subsequent pannings. Affinity-selected phagedisplayed peptides were obtained by competition assay after incubation at room temperature for 90 min with TsCa at a concentration 100 times higher than that of bovine IgG.</Brief_Description>
<BiopanningDataSet_Comments>The phage-displayed peptide VHTSIRPRCQPRAITPR competed with TsCa for binding sites, reducing the reactivity by approximately 30%.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2779</BiopanningDataSetID>
<Peptides>CPFPSPTWC[2.95 ± 0.07]
CFGLPSWAC[3.39 ± 0.28]
CNGFPSWC[3.34 ± 0.1]
CLGRPLWAC[3.17 ± 0.06]
CPHYSTLLC[4.07 ± 0.1]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25154906</Reference>
<Target_Name>Anti-soluble CD14-fraction ST monoclonal antibody</Target_Name>
<Template_Name>CD14</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>Affinities of phages to anti-soluble CD14-fraction ST monoclonal antibody were measured by phage ELISA. ELISA index values were read at 492 nm and data shown were reproduced from Fig. 1. An irrelevant peptide fused to a bacteriophage was used as a negative control, which had the value of 0.53 ± 0.08 when binding to the monoclonal antibody.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The competitive ELISA assay between M.H2 clone (CPHYSTLLC) and the recombinant sCD14 for binding to the polyclonal anti-CD14 antibody demonstrated its specificity to the target.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2780</BiopanningDataSetID>
<Peptides>CTPTFPPRC[2.35 ± 0.07]
CLNPVSSSC[2.52 ± 0.34]
CSTSSPSYC[1.62 ± 0.25]
CSLASLPAC[2.34 ± 0.18]
CTAQRLPSC[2.08 ± 0.13]
CTPLLSPFC[2.58 ± 0.2]
CSLLATAPC[2.76 ± 0.18]
CDHGPLPRC[2.78 ± 0.19]
CTLPVPLHC[2.99 ± 0.34]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25154906</Reference>
<Target_Name>Anti-CD14 polyclonal antibody</Target_Name>
<Template_Name>CD14</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>Affinities of phages to anti-CD14 polyclonal antibody were measured by phage ELISA. ELISA index values were read at 492 nm and data shown were reproduced from Fig. 1. An irrelevant peptide fused to a bacteriophage was used as a negative control, which had the value of 0.61 ± 0.12 when binding to the polyclonal antibody.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2781</BiopanningDataSetID>
<Peptides>LQWRRDDNVHNFGVWARYRL(2)
EEHTHRWPFWGHQERWGKQS(1)
EHGDGPGGKMRWWWHGGGTR(1)
GAFWKNNGSTQPWNPEDSSL(1)
GDATAKEMRSTQDTPQERGA(1)
LSLGRGADRIIPWELRRPGG(1)
MEGRSIGGRFRHTADMMVEA(1)
RVSGDNQAPTQRNNQGAEWT(1)
SQTLKGWRTGKLQPETLRWS(1)
SSEFAGENGGSTRGHKFDGY(1)
VAPLLRSESAIARSLVSYPQ(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. H1299 NSCLC cells of this group remains untreated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2782</BiopanningDataSetID>
<Peptides>AARPPTAPTEMHGAEMKGMT(1)
EEGGEVKGSAHASTDDTTRF(1)
GDMVPWAHPWEPWLGNKVEA(1)
GTYASVTRSHDRSGERIGDH(1)
KVQVERKEALGIQKIAVSRR(1)
LAGRQGPERSTVENNLSGTK(1)
NATWGKALRDYHRGVWSRVS(1)
SKSFALDGTPERYSRTLVRR(1)
VVSIPSTVGKGYPDSWAVRR(1)
WEGSEGTVESDNLQNKKGGK(1)
WGANQNRFAMAWAGATGASS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. This group is then incubated with H1299 NSCLC cells treated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2783</BiopanningDataSetID>
<Peptides>ATEPRKQYATPRVFWTDAPG(10)
LQWRRDDNVHNFGVWARYRL(1)
FGSWPTGWKARAYNDLPPAR(1)</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:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. H1299 NSCLC cells of this group remains untreated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2784</BiopanningDataSetID>
<Peptides>ATEPRKQYATPRVFWTDAPG(9)
AAPRLGGTQIKSESTKMGSD(1)
GAWEAVRDRIAEWGSWGIPS(1)
TWDGNEAERSPGSTGEDAAR(1)</Peptides>
<Motif></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:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. This group is then incubated with H1299 NSCLC cells treated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2785</BiopanningDataSetID>
<Peptides>ATEPRKQYATPRVFWTDAPG(6)</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:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. H1299 NSCLC cells of this group remains untreated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2786</BiopanningDataSetID>
<Peptides>ATEPRKQYATPRVFWTDAPG(6)</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:25188559</Reference>
<Target_Name>NCI-H1299 non-small cell lung cancer 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>X20 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Round 1 of panning is performed against H1299 nonsmall cell lung cancer cells. The output of round 1 is then split into two groups. This group is then incubated with H1299 NSCLC cells treated with chlorpromazine.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2787</BiopanningDataSetID>
<Peptides>RTEVPVLSFTSPLTG[1.76]
GDVWLFKTSTSHFAR[1.91]
AREYGTRFSLIGGYR[0.21]
HAAFEPRGDVRHTLL[2.00]
LGRAGQSYPSFARGL[0.52]
PIFPVVSSSGSSSSP[1.58]
PLSHGSVVYPRSSLG[1.36]
RRDTVPRSLSAPLSW[0.59]
PAVASTSSLIIDGPF[2.29]
HPPLASVWHVSVPL[0.83]
LHDFRSPIYASLLGF[1.53]
AGDGGLGRVAAGARV[1.15]
RVFHLWPHPTSTLSA[0.25]
APLSYNFASMPFMSG[0.73]
HPGWFDSAWFRAVSR[1.24]
ARDSRCGGFLGCGVT[1.36]
AMVRGFSFGMSRGSD[1.94]
RSLWSDFYASASRGP[6.57]
SYSVVNSPWCDGTCD[1.25]
SRDGLHSFCYVGCPP[0.40]
GVGDADGFIPVISAV[0.59]
PVFFRLSPVTEGGGV[1.40]
FPSYPFIAYSLQTPV[1.23]
RRLPHLMPFEGSVFL[3.55]
GPHFDYRTGLGWRFG[1.35]
LGKGLTGSALSLSAL[2.29]
YGVTPSPRSPWATAH[3.43]
VFVDGARYSTASDSL[2.83]
GAGIFGPWGVFAAVP[1.21]
GYRSAFVPFVARGGH[3.65]
RYRVGFTPGTIAAVL[1.13]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>31</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:25250205</Reference>
<Target_Name>Human ovarian adenocarcinoma cell line SKOV-3</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>f5-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method>Competition experiment,Micropanning assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Micropanning assay was used to determine binding of selected phage clones to SKOV-3 and HS-832 cells. SKOV-3 or HS-832 cells were incubated with individual phage clones and eluted using 2.5% CHAPS. Phage binding was determined by titer and the SKOV-3 to HS-832 ratio was calculated and shown. In addition, competitive binding experiments indicated that the peptide RSLWSDFYASASRGP displayed a half maximal inhibitory concentration (IC50) value of 10.5 ± 1.1 μM.</Affinity_Measurement_Description>
<Brief_Description>The library was pre-cleared from vasculature and non-tumor target binding phage according to previous methods. The pre-cleared phage library was screened against xenografted human OC SKOV-3 tumors in mice.</Brief_Description>
<BiopanningDataSet_Comments>In the last round of selection, 31 individual phage clones were identified, and that phage clone RSLWSDFYASASRGP exhibited the highest SKOV-3-to-HS832 binding ratios of 6.57, indicating preferable binding to the human OC cell line.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2788</BiopanningDataSetID>
<Peptides>VTVPTMPIRTAT
FTVPTVPITALH
ATVPTTPITLTP
GFTVPHLPIVPE
FIVPTIPIRGLP
SPGIHVVPTRPI
FPTYVPYAPIPP
VIVPVTPIKPQA
QPFVVPTSPVRG
HAVVPVNPVKSL
TALHYAPVPVGP
TPIFVQPWTPTY
VTVPTQEITPNL
SIFVPTHSIEPS
SVVPTVTITGNY
SVVPFHEIISRG
VSVPTVSIKPYI
KAVVPVSSIMPF
DSVTPTSVMAVA
YLQQDPLPRKTY
AYALPGPDPLPR
NVDQGRDPLPRE
WQNEDPLPRFSW
LSPLGGWDPLPR
KLDPLPRHFSAA
ITPGQWRSPLHF
LTPGQLNQQIWE
LTPGQITFTQGQ
LTPGQHLWWRSP
TPGQLRAESAMT
LTPGQAERWWAR</Peptides>
<Motif>VPTXPI, VTPXXI, DPLPR, LTPGQ</Motif>
<Unique_Sequence_Number>31</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:25273631</Reference>
<Target_Name>Anti-1/3NH2TTPI polyclonal antibody</Target_Name>
<Template_Name>Triosephosphate isomerase (EC:5.3.1.1)</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>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>Fourty-one phage mimotope clones were isolated and grouped according to their amino acid sequence, finding the consensus VPTXPI, VPTXXI, LTPGQ, and DPLPR.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2789</BiopanningDataSetID>
<Peptides>ADANRHSTLRER
TPLWQHLLSGRA
ADANRRSTLRER
TPPWVTVLLSRQ
ADSRRALLAQRA
TPQWQQLLSFRQ
ADSWRALLAQRA
TPSWATLLAQRA
ASPWHQLLAERR
TYRMDIMSIKTV
ATSWKEMLAERQ
WHDITSLRQYSF
DSPPIFDATLPK
TPWEEVLLSRLR
DWREILGARSQV
DPVWVNILTSRQ
EHVLWQQLLTSR
AQWQETLSERAR
ENWRLTLLQRNG
KCCYYDHSHALS
GGLHWTEILRSR
HSLRSDWPLRPG
GGVHWSEILSYR
ELTGWRLLLAQR
GRLQQHEIFRSG
KVVDLYSGWNRS
KTPWQEMLASRI
HVLWQHVVDLCR
PPMWADMLLARS
GPFLPLTSLHWR
SCKQVLEHRQGM
NWRETMGVRSQV
SIDGRSIISSRN
SDWTHVLSQRAL
SLDWTELLRLRT
KIYDLSLLHPST
SMPQWQELLKVR
QPAWQQTLINRS
SPLWQDIILTRS
SWMETLRTRNMS
SPTYHSSTGLND
SLSNYQIAGNGL
SSPSWRDVLLSR
TVSWQALLEMRQ
STGDWREILRNR
TPAWQATLLGRQ
TDWRTQLHLRQG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>47</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25301558</Reference>
<Target_Name>Enterobactin synthase component E</Target_Name>
<Template_Name>2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase</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>Upon panning immobilized EntE with a random peptide phage library, we recovered 47 unique EntE-binding dodecamer peptide sequences that aligned to a region of the EntA primary sequence corresponding to helix alpha 4.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2790</BiopanningDataSetID>
<Peptides>KVWLPPRHEHQY(2)[0.92 ± 0.03]
KVFYPAAANPNQ(1)[0.41 ± 0.06]</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:25311190</Reference>
<Target_Name>Vaccinia virus strain NYCBOH</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>Affinities of selected phages to vaccinia virus strain NYCBOH were measured by phage ELISA. The OD450-620 values were given and data shown were reproduced from the Fig. 1 in the reference. The wild-type M13KO7 phage (WT) was used as a control, which had the value of 0.3 ± 0.01 when binding to vaccinia virus strain NYCBOH.</Affinity_Measurement_Description>
<Brief_Description>A negative selection was performed before every biopanning round. In the negative biopanning, the library was added to BSA-coated wells. Then the supernatant was transferred to target-coated wells. After the fourth round, binding phages were eluted and used for a further negative selection against HEp-2 cell lysate.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2791</BiopanningDataSetID>
<Peptides>NRPDSAQFWLHH(3)[0.92 ± 0.06]
KVWLPPRHEHQY(1)[0.92 ± 0.03]
KVFYPAAANPNQ(1)[0.41 ± 0.06]
QALLEGNAKGGN(1)[0.91 ± 0.04]
TADKLLYGLFKS(1)[2 ± 0.05]
DEWDALLMRIRT(1)[1.39 ± 0.12]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25311190</Reference>
<Target_Name>Vaccinia virus strain NYCBOH</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>Affinities of selected phages to vaccinia virus strain NYCBOH were measured by phage ELISA. The OD450-620 values were given and data shown were reproduced from the Fig. 1 in the reference. The wild-type M13KO7 phage (WT) was used as a control, which had the value of 0.3 ± 0.01 when binding to vaccinia virus strain NYCBOH.</Affinity_Measurement_Description>
<Brief_Description>A negative selection was performed before every biopanning round. In the negative biopanning, the library was added to BSA-coated wells. Then the supernatant was transferred to target-coated wells. After the fourth round, binding phages were eluted and used for a further negative selection against HEp-2 cell lysate.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2792</BiopanningDataSetID>
<Peptides>NPTPYPMLPLRG(8)[0.52 ± 0.02]
GDLASWIITSFK(8)[1.87 ± 0.12]
TADKLLYGLFKS(6)[2 ± 0.05]
KIFQLPQISPPM(4)[1.11 ± 0.04]
TPVWSWEPPLQE(4)[1.93 ± 0.05]
KVWLPPRHEHQY(3)[0.92 ± 0.03]
DEWDALLMRIRT(3)[1.39 ± 0.12]
QALLEGNAKGGN(2)[0.91 ± 0.04]
KPTYSWDPAQLK(2)[0.98 ± 0.01]
GPTFSWDHLRGQ(2)[0.69 ± 0.02]
NMELHPHSLPRP(2)[0.61 ± 0.05]
ANTTKHSVLAAI(2)[1.2 ± 0.04]
EALNDWVNDSEY(2)[1.45 ± 0.06]
APTAYNKNDWAL(2)[0.95 ± 0.03]
DPWWRGNEARAA(2)[0.78 ± 0.02]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>15</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:25311190</Reference>
<Target_Name>Vaccinia virus strain NYCBOH</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>Affinities of selected phages to vaccinia virus strain NYCBOH were measured by phage ELISA. The OD450-620 values were given and data shown were reproduced from the Fig. 1 in the reference. The wild-type M13KO7 phage (WT) was used as a control, which had the value of 0.3 ± 0.01 when binding to vaccinia virus strain NYCBOH.</Affinity_Measurement_Description>
<Brief_Description>A negative selection was performed before every biopanning round. In the negative biopanning, the library was added to BSA-coated wells. Then the supernatant was transferred to target-coated wells. After the fourth round, binding phages were eluted and used for a further negative selection against HEp-2 cell lysate.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2793</BiopanningDataSetID>
<Peptides>CGGIALAGC(22)
CGWHRWRVC(3)
CLDLGVADC(2)
CLMRFQRSC(2)
CLHALRGRC(2)
CRTSLTGPC(2)
CLRMGFRSC(2)
CRFGSLVGC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:25324134</Reference>
<Target_Name>Surface glycoprotein Tc85-45</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>fUSE5-based CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>One hundred phage clones from the fifth round were randomly chosen and sequenced. Sequence alignment analysis revealed that 22 % of the phages encoded the peptide motif CGGIALAGC.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2794</BiopanningDataSetID>
<Peptides>CLPFRWTRC(7)
CRWPALLTC(4)
CWMMGPYFC(4)
CRLDSFNRC(3)
CGWHRWRVC(3)
CWGDVPSGC(3)
CSGFRVEAC(2)
CRFGSLVGC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:25324134</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>fUSE5-based CX7C 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>2795</BiopanningDataSetID>
<Peptides>LLSSKTL
LSFPFPG
FTSFSPY
QATHFHS
LASLPFR
THVFSWI
ACDPSPN
TPSLHRS
TAMARSA
VALLPHH
QSPPALL
FSLLGSL
VLLGPFP
YPFSLLH
SLGPQIK
MSPTYLL
DRAALSL
ALTPQLL
QTSPPLA
FPLFGLS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25333662</Reference>
<Target_Name>Sera IgG from asymptomatic CVL and symptomatic CVL</Target_Name>
<Template_Name>Leishmania infantum</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The phage library first incubated with IgGs from healthy dogs. The supernatant containing the clones that were not adhered to the IgGs was recovered and transferred to a new tube, and this procedure was repeated for three times. Then, the supernatant incubated with IgGs purified from asymptomatic CVL. The bound phage clones were transferred to a new tube containing the IgGs purified from asymptomatic CVL, and the process was repeated for three times. After this, the recovered phage clones were transferred to a new tube containing the IgGs that had been purified from symptomatic CVL, and the process was also repeated for three times.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2796</BiopanningDataSetID>
<Peptides>TGFFSQR[1.60]
VFGFFNTR[1.63]
TGFFATP[1.66]
MPGFFEMR[1.65]
NGYFARN[1.63]
SGYFSNN[1.69]
VGYFFER[1.63]
GFFATQ[1.70]
SGFFSDR[1.56]
SGYFAER[1.84]
SGFFESK[1.76]</Peptides>
<Motif>TGFFAKK</Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25468796</Reference>
<Target_Name>Anti-GapC monoclonal antibody 1E11</Target_Name>
<Template_Name>Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The binding activities of positive phage clones to mAb1E11 were measured by sandwich ELISA. The OD values at 405 nm were read and data shown were reproduced from the Fig. 1E in the reference. The wild-type M13 phage was used as a control, which had the value of 0.35 when binding to the mAb1E11.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Eleven positive clones recognized by mAb1E11 were identified, most of which matched the consensus motif TGFFAKK. Sequence of the motif exactly matched amino acids 97–103 of the S. dysgalactiae GapC.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2797</BiopanningDataSetID>
<Peptides>DHIHWITPSHPG[2.15 ± 0.09]
DHYSYTWFSWPT[1.55 ± 0.07]
ACSYHTTRAFVC[1.52 ± 0.12]
ACLYHTTRAFVC[1.73 ± 0.08]
GHFKWVPYDSLY[2.05 ± 0.1]
THWNWLNPYMAV[0.91 ± 0.15]
ALKIWPNPPRSN[1.13 ± 0.2]
WHLEWITPMASD[2.16 ± 0.05]
THISWMSPQKLW[1.46 ± 0.02]
THERLYWYSPSE[1.33 ± 0.2]
DSLRQLPLPVLS[1.44 ± 0.27]
EHMQWMRATDLF[1.73 ± 0.09]
QLEWSYWPQLSR[2.03 ± 0.06]</Peptides>
<Motif></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:25446106</Reference>
<Target_Name>3-hydroxy-3-methylglutaryl-coenzyme A reductase ( (EC:1.1.1.34))</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>Binding capabilities of the selected phages toward recombinant hHMGR was estimated by ELISA. The OD values at 655 nm were measured and data shown were reproduced from the Fig. 1 in the reference. The experiments were performed in triplicate and presented as mean ± standard deviation. The original library was served as the control, which had the value of 0.12 ± 0.02 when binding to the hHMGR protein.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These peptides are all hydrophilic in nature (negative values of xLogP), and most are negatively charged with approximately 30% hydrophobic residues. The results indicate that the tetrapeptide PMAS inhibits hHMGR effectively (IC50 = 68 μM), could be a lead compound to develop hypocholesterolemic agents.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2798</BiopanningDataSetID>
<Peptides>CTPAFRYSC(20/151)
CSSHSLLYC(9/151)
CGQHIERGC(9/151)
CAVLTHPAC(8/151)</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:25393207</Reference>
<Target_Name>Bone marrow-derived dendritic cell</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>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 the third round of biopanning, 151 phages were randomly isolated and analyzed for peptide sequence. Four phage isolates frequently appeared up to 30% of phages. Besides, CTPAFRYSC (TP) conjugated to chitosan in order to develop an efficient DC-targeting vaccine delivery carrier.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2799</BiopanningDataSetID>
<Peptides>TDHTHNKGYANK
TSHPSYYLTGSN
SHQALQEMKLPM
SMESLSKTHHYR
KLHISKDHIYPT
NRPDSAQFWLHH
DPQNHNWTNKPA
YLPHMLVHGSRH
TYPVVGHQQNVM
DIMPKLRDDVHN
NAHTSNNVVAFP
YGTSMTQSNWRH
SYGSLQTRFGHI
KFFNNTEATTRP
NYALRDPVGQRY
LPSVTEILGSNF
TSAVTLTSDPTL
QNFSQMMSIPRK</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:25343575</Reference>
<Target_Name>9-fluorenylmethoxycarbonyl-threonine and leucine-methyl ester (Fmoc-T/L-OMe)</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 biopanning process revealed 18 phage clones which are able to catalyze formation of the self-assembling reaction product in the second round of panning.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2800</BiopanningDataSetID>
<Peptides>AMHSLVGPAFNR
HDTSEQLLVAPS
DLRSCTACAVNA
ATTWTVAHGVSR
STDDDHLLAATT
HPTGSKSTTSTY
HTDSDPLLAAPS
PTSEVYLFSGNF</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:25343575</Reference>
<Target_Name>9-fluorenylmethoxycarbonyl-threonine and leucine-amide (Fmoc-T/L-NH2)</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 biopanning process revealed 8 phage clones which are able to catalyze formation of the self-assembling reaction product in the second round of panning.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>