<result><BiopanningDataSet><Item><BiopanningDataSetID>1526</BiopanningDataSetID>
<Peptides>DMPGTVLP</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:21050894</Reference>
<Target_Name>Human breast cancer cell line MCF-7</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>The phage DMPGTVLP (designated by the structure of the borne foreign peptide) demonstrates high selectivity and specificity towards target cells versus control unrelated cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1527</BiopanningDataSetID>
<Peptides>AHSLKSITNHGL(1)
GLNLPQNKVSFS(1)
GPSYLHRLVPAF(1)
LPDPHATNILFR(1)
SEAVRHLAGPPR(1)
SISTSFHAYKLK(1)
TGNYKALHPHNG(12)
TPQLPIDVNADR(1)
YLPDQQLTWFPS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21470674</Reference>
<Target_Name>ICR male mice brain</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>Phage Clone displaying Pep TGNYKALHPHNG revealed a significant superiority on brain transport efficiency compared  with native M13 phage. When conjugated on the surface of PLGA nanoparticles, Pep TGNYKALHPHNG facilitated the targeted delivery of nanoparticles across the BBB, leading to significant higher bEnd.3 cells uptake and in vivo brain accumulation.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1528</BiopanningDataSetID>
<Peptides>NLLNHPQ(2)
SLLAHPQ(1)
STHTSAQ(1)
SLIAHPQ(1)
TLLAHPQ(1)</Peptides>
<Motif>HPQ</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:21473586</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</Template_Name>
<Structure_of_Target_Template_Complex>1DF8,1LUQ,1MEP,1MK5,1N43,1N9M,1NDJ,1NQM,1STP,1SWD,1SWE,1SWG,1SWK,1SWN,1SWP,1SWR,1SWT,2F01,2GH7,2IZF,2IZG,2IZH,2IZI,2IZJ,2RTD,2RTE,2RTF,2RTG,2Y3F,3MG5,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method>ELISA,Surface plasmon resonance (SPR)</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The peptide SLLAHPQGGG-mpal was coupled via NCL to the fluorescein labeled EG linker and purified by prep-HPLC (yield = 60%). ELISA and Biacore measurements were performed. The ELISA (on a 100% SA packed
The peptide SLLAHPQGGG-mpal was coupled via NCL to the fluorescein labeled EG linker and purified by prep-HPLC (yield = 60%). ELISA and Biacore measurements were performed. The ELISA (on a 100% SA packed\r\nsurface) showed a Kd of 97 μM, while the Biacore measurements yielded 57 μM.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1529</BiopanningDataSetID>
<Peptides>AMYYPLWPSLVY(1)
APGYARLPSLMS(1)
AVGGQTPIRAKI(1)
AYSPISTVTQPY(1)
CPLPYPLCLPHG(1)
DAMIMKKHWHRF(1)
DLQALLPNYPRI(1)
ELTWPHVHRKPS(1)
ERQGTPYSMYVL(1)
FHKEWRTHFQQR(1)
FHKHSPRSPIFI(2)
FHKYPRPVAMTF(1)
FPKAFHHHKIYK(1)
GLLHHKHHRSPY(1)
GPLLVLNSHSFD(1)
GSAVASTLPLGQ(1)
HFKHQHSYARPP(1)
HFKYHHHMLRSP(1)
HFNHTIPLSANP(1)
HGSKHMPQQSTH(1)
HILPWKIPAHSA(1)
HILSPSGSPRMS(1)
HISPISAYPWVS(2)
HLPRHHWQWPSR(1)
HSFHSHVHLKNR(1)
HSYMPPLPPQLY(1)
IPHPHRWPLHSH(1)
IPTMPHPSTARE(1)
IQSGTPHPPLRS(1)
LEAPRPTPAVPM(1)
LHSSVQLTYPLP(1)
LITNNPGRLPPQ(1)
LLHAPYDHSVSP(1)
LSPLYPQLLGLA(3)
LTHNKMHREQAS(1)
LTYQPLFPTLVY(1)
NAISWFPMHLAH(1)
NISSIRPTLVEV(1)
NVHIRQPLGASS(1)
QHVQHQLASTGE(1)
QNNLDYIGLYAR(1)
QSMLGFISVSAK(1)
QTTTAPRHTLWL(1)
SAPYKPLLHHFG(1)
SHEIYVGSDGFR(1)
SHWWARVPFYPP(1)
SLVPSYHRSLST(1)
SMMMPDQLSLGR(1)
SMTHLYTDLWQP(1)
SPPTPHHPHPRL(1)
SPRTPDLTSLLP(1)
SSPFXWQSFSEV(1)
STAQPRFGPSSL(1)
SYSRTVPPAQWP(1)
TCPRYICQAPHP(4)
TLTWHTKTPVRP(1)
TNVPNPLQPNPR(1)
TTGLVQPTAIDP(1)
TTNIYFNTPAEV(1)
WHKHIPSPRASS(1)
WHKHPHAVFNAR(1)
WHQSWWAARLGQ(1)
WHSSWKSRVVPT(1)
YALKHLPESTIP(1)
YKAPRHLASHLF(1)
YPTSNIIPSIWS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>66</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21496351</Reference>
<Target_Name>AC3</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>In fact, the target is purified recombinant AC3 protein with Maltose Binding Protein as fusion tag (MBP-AC3).</Brief_Description>
<BiopanningDataSet_Comments>Few of these interacting peptides were found to be homologous to proteins from replication process, RNAi pathway, histone and DNA modifying enzymes indicating the role of AC3 in these pathways.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1530</BiopanningDataSetID>
<Peptides>TPITQLL(10)
QTSSAAL(4)
STFTTTL(4)
SLPLPKP(2)</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:21533529</Reference>
<Target_Name>The first and second extracellular loops of CCR5</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>These peptides could significantly protect against and reduce the severity of EAE. The infiltration of monocytes and lymphocytes into the spinal cord decreased significantly in treated mice, while abundant infiammatory cells and demyelination were observed in spinal cords of EAE mice.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1531</BiopanningDataSetID>
<Peptides>RRSHPCRTCTTHTP
HRKTTCTRCPATSP
HRRGECRACPLLPA
RRPAHCHHCPRNPL</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:21539876</Reference>
<Target_Name>Anti-PSA monoclonal antibody</Target_Name>
<Template_Name>Prostate-specific antigen, PSA</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-Cys2 phage display library (X5CX2CX5)</Library_Name>
<Affinity_Measurement_Method>Western blot</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In Western blot, peptide 1 (RRSHPCRTCTTHTP) antiserum recognized PSA protein where as peptides 2 (HRKTTCTRCPATSP), 3 (HRRGECRACPLLPA) and 4 (RRPAHCHHCPRNPL) does not.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These peptides apart from differences in their amino acid sequence, elicited minimal cross reactive antibody responses against each other. One of the four peptides analyzed produced an antibody response that recognizes the PSA protein.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1532</BiopanningDataSetID>
<Peptides>AQSPTIKLTPSW(1)
ANSYSVNYTPSM(1)
SVSVGMKPSPRP(7)
ESSYSWSPARLS(1)
KPFHDWLYSPTA(1)
ATPHYTVGQWNQ(3)
NHNMHRTTQWPL(1)
LPNIPYHHPLYH(1)
SDIRNWDTQSLP(2)
SDIWPLQSQMYP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21544611</Reference>
<Target_Name>Human ovarian tumor cell line SK-OV-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>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Cells were washed twice with serum-free medium, and re-incubated in serum-free medium for 2 h at 37 ℃ to clear their surface receptors.', '3', '21544611', 'The synthetic biotin-labeled peptide, SVSVGMKPSPRP, demonstrated a high specificity to SK-OV-3 cells especially when compared to other cell lines (A2780 and 3T3).</Brief_Description>
<BiopanningDataSet_Comments>The synthetic biotin-labeled peptide, SVSVGMKPSPRP, demonstrated a high specificity to SK-OV-3 cells especially when compared to other cell lines (A2780 and 3T3).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1533</BiopanningDataSetID>
<Peptides>STLPLPP(9)
SPMTLYG(6)
TMQMTRY(6)
LVTTGPL(4)
QTHSWWP(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21567665</Reference>
<Target_Name>Lead Ion, Pb(2+)</Target_Name>
<Template_Name>Imidazol</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>Bound phages were eluted with 200 mM imidazol solution.</Brief_Description>
<BiopanningDataSet_Comments>Isothermal calorimetric analysis revealed that the peptide STLPLPP bound to Pb(2+), Cd(2+), Hg(2+), and Cu(2+). Through the use of CD studies, no secondary structural changes were observed for the peptide upon binding to divalent cations. Ala scanning mutant peptides bound to Hg(2+) with a reduced affinity. However, no single substitution was shown to affect the overall affinity.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1534</BiopanningDataSetID>
<Peptides>GRQYYEGRKPDYRAA(18)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:21573118</Reference>
<Target_Name>Anti-HMW-MAA monoclonal antibody VT80.12</Target_Name>
<Template_Name>High molecular weight melanoma-mssociated antigen, HMW-MAA</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 PC89 phage diaplay library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In ELISA inhibition experiments, the peptide GRQYYEGRKPDYRAAC inhibited the binding of the mAb VT80.12 to the HMW-MAA up to 93%.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Twenty individual phage clones were tested for their ligand specificity in phage ELISA. Among these, eighteen phage clones specifically bound to the mAb VT80.12. DNA sequencing of these 18 phage clones yielded one peptide sequence GRQYYEGRKPDYRAA. Peptide inhibited the binding of mAb VT80.12 to the HMW-MAA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1535</BiopanningDataSetID>
<Peptides>GRQYYEGRKPDYRAA(19)</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:21573118</Reference>
<Target_Name>Anti-HMW-MAA monoclonal antibody VT80.12</Target_Name>
<Template_Name>High molecular weight melanoma-mssociated antigen, HMW-MAA</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 PC89 phage diaplay library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In ELISA inhibition experiments, the peptide GRQYYEGRKPDYRAAC inhibited the binding of the mAb VT80.12 to the HMW-MAA up to 93%.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Twenty individual phage clones were tested for their ligand specificity in phage ELISA. Among these, nineteen phage clones specifically bound to the mAb VT80.12. DNA sequencing of these 19 phage clones yielded one peptide sequence GRQYYEGRKPDYRAA. Peptide inhibited the binding of mAb VT80.12 to the HMW-MAA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1536</BiopanningDataSetID>
<Peptides>NYQDLQRTHFKS(20)</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:21573118</Reference>
<Target_Name>Anti-HMW-MAA monoclonal antibody VF1-TP43</Target_Name>
<Template_Name>High molecular weight melanoma-mssociated antigen, HMW-MAA</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 ELISA inhibition experiments, the peptide NYQDLQRTHFKSGPGPGC inhibited the binding of the mAb VF1-TP43 to the HMW-MAA up to 100%.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Among 30 tested phage clones, 20 were specifically recognized by the mAb VF1-TP43 in phage ELISA. DNA sequencing yielded one peptide sequence NYQDLQRTHFKS. Peptide inhibited the binding of mAb VF1-TP43 to the HMW-MAA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1537</BiopanningDataSetID>
<Peptides>WHWTYYW(39)
THKFPWI(1)
WHWLWLQ(1)
HLPPNHT(1)
KLWTIPM(1)
SSLRLLP(1)</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:21592685</Reference>
<Target_Name>Major outer membrane protein</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>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>To identify host proteins that interact with LipL32, phage display technology was employed in the study. The nucleotide and corresponding peptide sequences from pyrosequencing were analyzed and used to search for matched host proteins in the protein databases using the BLASTP program of National Center for Biotechnology Information (NCBI). Putative proteins with potential binding to LipL32 are proteins known to be expressed on the surface of target cells of pathogenic Leptospira such as chloride channel accessory 2, glycoprotein VI, scavenger receptor expressed by endothelial cell isoform I (SREC-I), coronin 2A, laminin alpha 5, collagen XX, and prostaglandin receptor EP1.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1538</BiopanningDataSetID>
<Peptides>IYSNTSAPHLII(2)[1.294 ± 0.245/1.754 ± 0.258]
LTRGYNTSLFQE(1)[1.986 ± 0.189]
GHTLNAPINLPM(1)[1.621 ± 0.094]
ALHMKLGPQYYP(1)[1.513 ± 0.139]
LTNQLQHTWISP(1)[3.308 ± 0.303]
SATMGRVPTTAS(1)[1.318 ± 0.126]
YHETRIIEGADS(1)[1.268 ± 0.120]
NTPSPYPMSSAP(1)[1.558 ± 0.107]
VFRDVTPMLLTY(1)[2.648 ± 0.037]
MNYMNITISVEK(1)[1.891 ± 0.132]
KIMPPNWLVAKL(1)[2.270 ± 0.258]
NFTSHDFWFWMT(1)[2.824 ± 0.283]
NDPNNVNPTAGR(1)[1.513 ± 0.227]
KYLAYPDSVHIW(1)[3.371 ± 0.202]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3-4</Rounds_of_Panning>
<Reference>PMID:21611873</Reference>
<Target_Name>LNCaP prostate carcinoma 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>Binding of the selected phages on LNCaP and PC-3 cells was examined with cell phage ELISA. OD450(LNCap)/OD450(PC-3) was reproduced from the graph and shown. Results are represented as the mean ± SD (n=3). The value of the insertless phage was 0.979 ± 0.397.</Affinity_Measurement_Description>
<Brief_Description>Biopanning were performed on LNCaP cells after pre-cleaning on PC-3 cells to remove the non-specific bound phages.</Brief_Description>
<BiopanningDataSet_Comments>Cell  phage  ELISA  and  immunostaining demonstrated high specificity of phage clone (KYLAYPDSVHIW) to LNCaP cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1539</BiopanningDataSetID>
<Peptides>MPKDMLPYANPN
QSFKDHLPAGMR
HSFEPWSARDML
NMSLRDHYSPSP
WSPSKLYSARDH
THRPLSHNFRDF</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.5 monoclonal antibody H12H3</Target_Name>
<Template_Name>Variable surface glycoprotein 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>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP. Bound phages were eluted via antigen competition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1540</BiopanningDataSetID>
<Peptides>ALLPFKDHLPYP
APQNAKDHLPGY
APWSLRDHLAVT
FAENKKDHFSPG
QPNHRDHFKLPA
TPGVERDHFVRL
SLMHVYRDHSTS
SNWRDHYGLGAG
MQDSRLRLALSA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.5 monoclonal antibody H12H3</Target_Name>
<Template_Name>Variable surface glycoprotein 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>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1541</BiopanningDataSetID>
<Peptides>CWPSMRDHC
CTYSPRDMC
CRDHFSTHC
CRDHYPLSC
CKDHATDLC
CISPNQWLC
CTSPNQWLC
CLDAKLQQC
CPNFELHWC
CPPYETWWC
CNVYEAYWC
CTDFEGMLC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.5 monoclonal antibody H12H3</Target_Name>
<Template_Name>Variable surface glycoprotein 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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1542</BiopanningDataSetID>
<Peptides>CWYSTRDHC
CRDHYDQMC
CRDHSDLWC
CRDHLYGSC
CKDHATDLC
CWALRDPLC
CNALNQWLC
CRTSNQWLC
CTALQQWLC
CLDAKLQQC
CQMPHWWHC
CQVPHFFGC</Peptides>
<Motif></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:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.5 monoclonal antibody H12H3</Target_Name>
<Template_Name>Variable surface glycoprotein 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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP. Bound phages were eluted via antigen competition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1543</BiopanningDataSetID>
<Peptides>MDWINPFPNFNS
RVPNVLPLFPFL
NSPFMLHMSALS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.3 monoclonal antibody H13F7</Target_Name>
<Template_Name>VSG 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>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1544</BiopanningDataSetID>
<Peptides>QPAIWINPFPAW
TPSWRNPFPTFY
LTPPPWQNPFPP
AHPPWPLQYVFR
TPTWPLLTIFPS
NSPFMLHMSALS
SELSPAMLHFMF</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.3 monoclonal antibody H13F7</Target_Name>
<Template_Name>VSG 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>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP. Bound phages were eluted via antigen competition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1545</BiopanningDataSetID>
<Peptides>CWLPLTRLC
CWHPLQWRC
CLEILSWLC
CNQVLSWLC
CILPWKHIC
CVLPWSHVC
CFLPHPSRC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.3 monoclonal antibody H13F7</Target_Name>
<Template_Name>VSG 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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP. Bound phages were eluted via antigen competition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1546</BiopanningDataSetID>
<Peptides>SHSTPYYWKGYI</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21695105</Reference>
<Target_Name>Anti-VSG LiTat 1.3 monoclonal antibody H18C11</Target_Name>
<Template_Name>VSG 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>Pannings were performed in the first two rounds consisting of 1) a positive selection with anti-VSG mAbs coated on magnetic particles (MP), 2) a negative selection with anti-VSG mAb-free MP. Bound phages were eluted via antigen competition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1547</BiopanningDataSetID>
<Peptides>FHWSWYTPSRPS(2)[0.579/0.354]
WHWPWYQGQLWP(2)[0.336/0.270]
SHWIDWLYSSPI(1)[0.169]
QHWYLWNLMYGA(1)[0.428]
WHWQYTPWWRGS(1)[0.610]
WHWQWTPWSIQP(1)[0.480]
FHWTQYFSPWIR(1)[0.597]
WHWSLYPLTYPP(1)[0.318]</Peptides>
<Motif>[AVLIFYW]-H-W-x-[AVLIFYW]-[AVLIFYW]-x-[AVLIFYW]-x-[AVLIFYW]</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:21713010</Reference>
<Target_Name>Human antimicrobial peptide LL-37</Target_Name>
<Template_Name>Glucan 1,3-beta-glucosidase</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 450 nm was determined using an ELISA reader. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description>LL-37 samples were added to the wells and incubated temperature to elute the bound phage.</Brief_Description>
<BiopanningDataSet_Comments>Using phage display and ELISA, authors identified 10 peptide sequences that could bind LL-37. A BLAST search revealed that four sequences in the major C. albicans cell-wall b-1,3-exoglucanase, Xog1p, were highly similar to the consensus sequence derived from the 10 biopanned peptides. One Xog1p-derived peptide, Xog1p 90-115, and recombinant Xog1p associated with LL-37, thereby reversing the inhibitory effect of LL-37 on C. albicans adhesion. LL-37 reduced Xog1p activity and thus interrupted cell-wall remodeling.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1548</BiopanningDataSetID>
<Peptides>STTPQSVYASAP(1)
AVPLNTSVLHTT(1)
PMPSNRPGYNVS(1)
YGCNTTPCHWAM(1)
GRLDDHNQSRML(1)
NTSHEILWQTYP(1)
SHGTLQRVHTWS(1)
DWRVIIPPRPSA(2)
AAFTPRPWPSTV(1)
YDESTYHQGQKR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:21624651</Reference>
<Target_Name>Rabbit chondrocyte</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>In the negative selection procedure, the phage display library was incubated with the synovial tissue and fluid to exclude the synovial affinity phage clones.</Brief_Description>
<BiopanningDataSet_Comments>Analysis suggests that the peptide DWRVIIPPRPSA can efficiently interact specifically with chondrocytes without any species specificity. Polyethylenimine (PEI) was covalently modified with CAP to construct a non-viral vector for cartilage-targeted therapy.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1549</BiopanningDataSetID>
<Peptides>DWRVIIPPRPSA(12)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:21624651</Reference>
<Target_Name>Rabbit chondrocyte</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>In the negative selection procedure, the phage display library was incubated with the synovial tissue and fluid to exclude the synovial affinity phage clones.</Brief_Description>
<BiopanningDataSet_Comments>Analysis suggests that the peptide DWRVIIPPRPSA can efficiently interact specifically with chondrocytes without any species specificity. Polyethylenimine (PEI) was covalently modified with CAP to construct a non-viral vector for cartilage-targeted therapy.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1550</BiopanningDataSetID>
<Peptides>LRSRTKIIRIRH</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:21596749</Reference>
<Target_Name>Heparan sulfate, HS</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>Viral entry and glycoprotein D binding assays together with fluorescent microscopy data indicated that peptide LRSRTKIIRIRH was potent in blocking HSV-1 entry into primary cultures of human corneal fibroblasts and CHO-K1 cells transiently expressing different glycoprotein D receptors.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>