<result><BiopanningDataSet><Item><BiopanningDataSetID>1951</BiopanningDataSetID>
<Peptides>HYDRHNYHWWHT(7)
LSKNLPLTALGN(1)
SGMKEPELRSYS(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:22424885</Reference>
<Target_Name>Anti-SapA monoclonal antibody A2D5</Target_Name>
<Template_Name>S-layer 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>15 phage clones were randomly chosen and tested for reactivity with mAb A2D5 by indirect ELISA. Single-stranded DNA from positive clones was sequenced and compared with the sequence of SapA to predict the key epitope. ELISA and/or Western blot analyses further validated that synthetic peptides and recombinant peptide mimotopes all interact with mAb A2D5. Nine of ten positive phage clones identified by screening were sequenced successfully. Seven clones shared the same sequence HYDRHNYHWWHT; one had the sequence LSKNLPLTALGN; and the final one had the sequence SGMKEPELRSYS. These three sequences shared high homology with SapA J05577 in the region GNEKDFVTKIYSIALGNTSDVDGINYW, in which the underlined amino acids may serve as key residues in the epitope.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1952</BiopanningDataSetID>
<Peptides>CPIKTLPMC(18)</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:22426388</Reference>
<Target_Name>Beta-amyloid protein 42</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>To confirm further the binding of XD4 (CPIKTLPMC) to Aβ42, Aβ42 or XD4 at different concentrations was coated onto ELISA plates. Subsequently, the phages expressing XD4 peptide, His tag conjugated XD4, or Aβ42 were added to the wells for ELISA measurement. The results showed that the phages and His tag-conjugated XD4 bound to Aβ42 in a dose-dependent manner. Conversely, Aβ42 also bound to coated XD4 in a concentration-dependent manner.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Thirty individual positive clones binding to Aβ42 with higher phage ELISA values were selected and amplified. The DNA from these 30 positive clones was extracted and sequenced. The level of consensus of the sequences was examined. The results indicated that 18 clones possessed the same sequence (PIKTLPM, denoted as XD4). XD4 significantly inhibited Aβ cytotoxicity, increased the microglial phagocytosis of Aβ, decreased the Aβ-induced generation of ROS and NO, and attenuated the disequilibrium of calcium homeostasis in vitro. Remarkably, XD4 also attenuated memory deficits in β-amyloid precursor protein/presenilin 1 (APPswe/PS1dE9) transgenic mice, and reduced amyloid plaque burden and Aβ40/42 levels.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1953</BiopanningDataSetID>
<Peptides>EMPWSTNSFTDD(1)
THQNNTSSLLGF(1)
ARLHMASTASSL(1)
YSDWQASTSSRL(1)
HQSISPSTSSKL(1)
THQHSTNSYLLL(1)
IMNSTSSFSHFQ(1)
AESTSSFKSPHH(1)
YASMLHSTSSKL(1)
SAGPSTSSELSS(1)
DYNRLNSTSSAL(1)
ERPSAVNTSSWL(1)
GYMEDANTTSKL(1)
DMSLSSSTSSLL(1)
RADMPSTSSALS(1)
FTNTTSFLVART(1)
TLTYAPSTSSPL(1)
STKLNSTSSTLG(1)
HKNLSNSTASLL(1)
ENHTHSNTSSAL(1)
LNSTVSFLQRSP(1)
SMYSTSSTLWAD(1)
THRYNSTSSLLT(1)
QYSTSSSLGISI(1)
DSRPSPSTSSHL(1)
YPSDWTSTSSML(1)
SPTHALSTSSQL(1)
VPIEAKSTSSFL(1)
FTWNHASTASFA(1)
FMTIEASTASSL(1)
ESLTNNSTASHL(1)
VSPHMMSTASAL(1)
QGWSTSSFTTRP(1)
SNQVVHQHSTLS(1)
TLNQHNTSSSLG(1)
SPPARSSTSSQL(1)
TSGQSTASHLLL(1)
IQPYASTSSALW(1)
TSPHGQSTSSFT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>39</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22427942</Reference>
<Target_Name>Anti-MSP1a monoclonal antibody 15D2</Target_Name>
<Template_Name>Major surface protein 1a, MSP1A</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 consensus sequence SxSSQSEASTSSQLGA was obtained, which is located in C-terminal end of the 28-aa repetitive motif of the MSP1a protein, but the alignment and sequences' variation among mimotopes allowed us to map the critical motif STSSxL within the consensus sequence.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1954</BiopanningDataSetID>
<Peptides>ATKVKIPFEAKV
VATPVPPTLTPF
ATLRTYPYMDRA
QLAPMATHDKHP
YALRPGMPQWLE
TPPTYSWFTHRM
GSATNPTMGQRM
AETHVLNKHTPL
HSSSHWSWSTPL
NMRLLANPAMAG
QIPAQNRLVFLT
VPGWDSHNARHQ
HAESPFPNPTRA
NKITLHSNSSIA</Peptides>
<Motif></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:22428072</Reference>
<Target_Name>Human corneal epithelial 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></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Fourteen sequences were obtained and BLASTp analysis showed that most of their homologue counterparts in GenBank were for defined or putative proteins in various pathogens.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1955</BiopanningDataSetID>
<Peptides>RKRIRRMMPRPS(5)
TNLKSIRRPQIP(2)
LRKRNNPIRTKM(1)
SSTRMISIRQST(1)
KMPRQSNRRLMM(1)
RHLQTSPIMLQI(1)
RHTNSTRLNRPT(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>PMID:22459587</Reference>
<Target_Name>Thiacloprid</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>1956</BiopanningDataSetID>
<Peptides>RNRHTHLRTRPR(6)
RRPKRKHRMHLS(2)
ISKHTPLRTRPR(1)
RRPKRQHTMQLS(1)
SMRMRIHIPSSH(1)
RQIIQPSPKQRR(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:22459587</Reference>
<Target_Name>Imidacloprid</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>1957</BiopanningDataSetID>
<Peptides>YNTNHVPLSPKY(20)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>7</Rounds_of_Panning>
<Reference>PMID:21209841</Reference>
<Target_Name>Extracellular domain of human carbonic anhydrase IX</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>Immobilized recombinant extracellular domain of the epidermal growth factor receptor (EGFR) was used for negative selection.</Brief_Description>
<BiopanningDataSet_Comments>After 7 selection rounds, single-stranded DNA from isolated bound phages was sequenced. All 20 clones sequenced, displayed the same peptide sequence: YNTNHVPLSPKY (CaIX-P1). In vitro binding experiments of 125I-labeled-CaIX-P1 revealed an increased uptake of the radioligand in the CAIX positive renal cell carcinoma cell line SKRC 52. Binding of the radioligand in the colorectal carcinoma cell line HCT 116 increased with increasing cell density and correlated with the mRNA expression of CAIX. Radioligand uptake was inhibited up to 90% by the unlabeled CaIX-P1 peptide, but not by the negative control peptide octreotide at the same concentration. No binding was demonstrated in CAIX negative CaKi 2 and HUVEC cells. Organ distribution studies revealed a higher accumulation in SKRC 52 tumors than in heart, spleen, liver, muscle, intestinum and brain, but a lower uptake compared to blood and kidney. These data indicate that CaIX-P1 is a promising candidate for the development of new ligands targeting human carbonic anhydrase IX.
</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1958</BiopanningDataSetID>
<Peptides>VDQNAKSWGQMK(1)
QSYSAKMWGQVG(1)
STDIISWKHWGS(2)
EHWPQWGLALKR(2)
TNLETLKQWGFP(1)
GNPAPWKDWGSA(3)
QSDKHWGMATPP(1)
DFYSWKHWGSTT(1)
YDNKEWGIARPN(1)
TPPPTYKLWGAL(1)
SSSKTWGAPLYY(1)
SSNDTKAWGFAV(1)
DYRSWGAVPLQL(1)
NSSSNKHWGSVP(1)</Peptides>
<Motif>KXWG</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:21233208</Reference>
<Target_Name>Anti-D2NS1 monoclonal antibody DB16-1</Target_Name>
<Template_Name>Non-structural protein 1, NS1</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 B-cell epitope of DB16-1 displayed a consensus motif, Lys-X-Trp-Gly (KXWG), which corresponded to amino acid residues 116-119 of DV NS1 and mimicked amino acid residues 334-337 in LYRIC. Moreover, the binding activity of DB16-1 in NS1 of DV-2 and in LYRIC disappeared after the KXWG epitope was deleted in each. In conclusion, DB16-1 targeted the same epitope in DV NS1 and LYRIC protein on human endothelial cells, suggesting that it might play a role in the pathogenesis of DHF/DSS.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1959</BiopanningDataSetID>
<Peptides>APSPMIW(5)
LQNAPRS(3)
HAIYPRH(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:18931708</Reference>
<Target_Name>CD133 extracellular fraction</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>In the screening, the phage display peptide library was subjected to three rounds of affinity selection. Each affinity selection was done by biopanning on ELISA plate. ELISA plates were blocked with bicarbonate buffer (PH 8.6) containing 50 mg/l streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1960</BiopanningDataSetID>
<Peptides>LVGVFH(0.8)</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:22452335</Reference>
<Target_Name>Porcine ear skin</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Skin was sandwiched between the donor and receptor compartments with the SC facing the donor compartment. Phages, from phage display peptide library (PDL) were loaded into the donor compartment of the Franz diffusion cell. The donor compartment was covered with parafilm to maintain occlusive conditions. Phage particles that crossed the skin were collected from the receptor chamber after 24 h and were amplified. An amplified pool of phages was loaded again in the donor chamber for another round of screening. In this way, screening was performed three times.</Brief_Description>
<BiopanningDataSet_Comments>Eighty percent of the phages that consistently crossed the porcine skin possessed T2 peptide (LVGVFH) on their surface. Pretreating the skin with synthetic T2 peptide at pH 4.5 resulted in significant penetration enhancement of hydrophilic drug 5-fluorouracil (5-FU) across skin. FTIR spectroscopy showed that the T2 peptide interacted with skin lipids to enhance the skin penetration. Pretreating the skin with T2 peptide enhanced the partitioning of small molecules with different lipophilicities (5-FU, fluorescein isothiocyanate, and rhodamine 123 hydrochloride) into skin. Fluorescence studies showed that T2 peptide enhanced the diffusion of these molecules into intercellular lipids of SC and thus enhanced the penetration into the skin. Histidine at the c-terminus of T2 peptide was identified to be critical for the skin penetration enhancement. T2 peptide interacted with skin lipids to cause skin penetration enhancement.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1961</BiopanningDataSetID>
<Peptides>GEVGEQEKARVG(1)
EGKGVEAVGDGR(2)
AEPDATGWRSLG(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:22484444</Reference>
<Target_Name>Chitin</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>SUT12 M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Based on phage ELISA results, Four phage clones showed binding signals two times higher than the background. The synthetic chitin binding peptide (ChiBP) could bind to chitin beads and disrupt their structure. This selected peptide was successfully used to immobilize alkaline phosphatase on chitin. In addition, the peptide could induce colloidal chitin in water to form a chitin coat on the surface of plastic tubes. Scanning electron microscopy (SEM) revealed that the peptide could induce colloidal chitin and chitohexaose to form networks when the temperature was raised to 42 ℃.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1962</BiopanningDataSetID>
<Peptides>AETVESCLAKSH(1)
ALNWASKSSGRY(2)
ANYFLPPVLSSS(2)
HPVLHLPISTPR(1)
ILPVQGIAMRSM(1)
LTPTVRSGYLNH(1)
MKPGQLRTGSTM(1)
MTEGMNRSQLPA(1)
NDSSSALPHTLT(1)
NHVHRMHATPAY(2)
NIYSTELAAPSP(1)
NLILTPGWSRLA(1)
NMFGSLTSHVTA(1)
NWELQSTPSHTA(1)
SKHFNPGLATAD(1)
SQLFITCPPISL(1)
SQLSITSPPISL(3)
TAMTQRISAGNH(2)
VATVMTTSAFEP(1)
WHWNLWAPASPT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>26</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22515661</Reference>
<Target_Name>Type IV secretion system protein virB8</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 authors have pursued an unbiased approach using peptide arrays and phage display to identify interaction partners and interaction domains of type IV secretion system assembly factor VirB8. These approaches identified the globular domain from the VirB5 protein to interact with VirB8. This interaction was confirmed in cross-linking, pull-down, and fluorescence resonance energy transfer (FRET)-based interaction assays. In addition, using phage display analysis, the authors identified different regions of VirB6 as potential interaction partners of VirB8.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1963</BiopanningDataSetID>
<Peptides>CLPSTNAMC
CLSTLRSTC
CNRLILPHC
CTTAQLRWC
CLHRHSQLC
CNPQPVAAC
CWQNKALAC
CYQTISAAC
CTSMKAAIC
CSLGSTIVC
CKFTLSLSC
CRHALNTAC
CLSAGGAEC
CSLGSTIVC
CYQTISAAC
CTILSGSRC
CLSAGGAEC
CKFTLSLSC
CTSMKAAIC
CYQTISAAC
CLSAGGAEC
CLSTLRSTC
CSLTALHRC
CTTAQLRWC
CKLLYYVSC
CPGLSAGRC
CLPSTNAMC
CLTAWGWAC
CSLGSTIVC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>29</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22515661</Reference>
<Target_Name>Type IV secretion system protein virB8</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>The authors have pursued an unbiased approach using peptide arrays and phage display to identify interaction partners and interaction domains of type IV secretion system assembly factor VirB8. These approaches identified the globular domain from the VirB5 protein to interact with VirB8. This interaction was confirmed in cross-linking, pull-down, and fluorescence resonance energy transfer (FRET)-based interaction assays. In addition, using phage display analysis, the authors identified different regions of VirB6 as potential interaction partners of VirB8.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1964</BiopanningDataSetID>
<Peptides>WAETWPLAQRPP(1)
DFRWATHMHTPA(6)
GTPPMSPQVSRV(1)
HFRWANHTHFQT(1)
TSQYQSPRAVHP(1)
HFRWANHTHFQT(1)
GLRNSVPYQTFT(1)
HFRWANHTHFQT(1)
GHGLLQYTDVMF(1)
QHTYWPNYTPLL(1)
HTRRTTHHILR(1)
APIKAPTIRDTA(1)
SKFEPISKYLQP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22536790</Reference>
<Target_Name>Major prion protein, PrP</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>Lyophilized streptavidin 1.5 mg (Ph.D.-12, BioLabs, New England) was dissolved in 1 mL of 10 mM sodium phosphate (pH 7.2) in 100 mM NaCl. For each target three wells of a 96-well plate were coated with the prepared solutions, i.e., 150μL/well overnight at 4°C under gentle agitation.</Brief_Description>
<BiopanningDataSet_Comments>The prion-targeting peptide P9 (WAETWPLAQRPP) shows homology to prion protein aa 16-28, i.e., WSDLGLCKKRPK. Prion-targeting peptide P50 (DFRWATHMHTPA) matches the identified prion consensus sequence as described in the text (X1FRWAX6HX8HX10X11X12), showing homology to prion protein aa 147?155, i.e., DRYYRENMHRYP.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1965</BiopanningDataSetID>
<Peptides>HLNILSTLWKYR(1)</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:22536790</Reference>
<Target_Name>Ganglioside GM1</Target_Name>
<Template_Name>Cholera toxin B protein, CTB</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>Lyophilized streptavidin 1.5 mg (Ph.D.-12, BioLabs, New England) was dissolved in 1 mL of 10 mM sodium phosphate (pH 7.2) in 100 mM NaCl. For each target three wells of a 96-well plate were coated with the prepared solutions, i.e., 150μL/well overnight at 4°C under gentle agitation.</Brief_Description>
<BiopanningDataSet_Comments>The authors show that the prion-targeting peptides do not induce efficient transcytosis of polymersomes across the BBB in vitro nor induce accumulation of polymersomes in the brain in vivo. In contrast, the G23 peptide is shown to have transcytotic capacity in brain endothelial cells in vitro, as well as a brain-targeting potential in vivo, as reflected by the accumulation of G23-polymersomes in the brain in vivo at a level comparable to that of RI7217-polymersomes, which are targeted toward the transferrin receptor. Thus the G23 peptide seems to serve both of the requirements that are needed for efficient brain drug delivery of nanocarriers. An unexpected finding was the efficient accumulation of G23-polymersomes in lung. In conclusion, because of its combined brain-targeting and transcytotic capacity, the G23 peptide could be useful in the development of targeted nanocarriers for drug delivery into the brain, but appears especially attractive for specific drug delivery to the lung.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1966</BiopanningDataSetID>
<Peptides>AADNAKTKSFPV(12)
IVWPTSPRALDA(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22563192</Reference>
<Target_Name>Human gastric cancer specimens</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>For screening, non-specific binding phage was cleared from the library by panning against normal appearing gastric mucosa adjacent to the tumor. Approximately 92.8% of the non-specific phage clones were subtracted from the original phage library after two rounds of biopanning against normal appearing gastric mucosa.</Brief_Description>
<BiopanningDataSet_Comments>The values for AAD peptide were statistically significant (P &lt; 0.01) for gastric cancer as compared with other histological classifications and control peptide. The peptide AAD identified in this study has the potential to guide tissue biopsy and improve the detection of pre-cancerous lesions in gastric mucosa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1967</BiopanningDataSetID>
<Peptides>CYWELEWAPC</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:22578098</Reference>
<Target_Name>Cardiac phospholamban, PLB</Target_Name>
<Template_Name>Sarcoplasmic/endoplasmic reticulum calcium ATPase 2, SERCA2, SR Ca(2+)-ATPase 2</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>CX8C fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Panning steps of the primary library were performed on 10-mm multiwell plates coated with streptavidin essentially. The target was the 36-PLB-C peptide biotinylated on the cysteine residue. Three enrichment cycles (e12 phage particles used in the first round, then 20% of the volume of the amplified eluates were used in the second and third rounds) were carried out.</Brief_Description>
<BiopanningDataSet_Comments>Its functional activity was tested in Ca2+ uptake assays utilizing preparations from cardiac sarcoplasmic reticulum. By synthesizing and testing a series of alanine point-mutated cyclic peptides, the authors identified which amino acid was important for the inhibition of the phospholamban function. The structures of active and inactive alanine-mutated cyclic peptides, and of phospholamban (1-36), were determined by NMR. This structure-activity analysis allowed building a model of phospholamban-cyclic peptide complex.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1968</BiopanningDataSetID>
<Peptides>SLTNLSK(16)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22588916</Reference>
<Target_Name>Human osteosarcoma MG-63 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.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Human embryonic kidney 293T cells was used to carry out subtractive panning.</Brief_Description>
<BiopanningDataSet_Comments>The sequence SLTNLSK was confirmed as the most frequent peptide by DNA sequencing and showed strong specificity verified by cell ELISA, fluorescent staining and organ immunohistochemistry.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1969</BiopanningDataSetID>
<Peptides>HLPLFRHVWPNM(1)
HLSTWLSHSWLR(1)
HLRQTLWNLSTS(1)
HWWQWPSSLQLR(1)
HNWTRWLLHPDR(1)
HWFSAWYQLGSN(1)
HWKPWWFSPGSW(1)
HWWHFYQPPLST(1)
HFSWFLPWNAPL(1)
HFTWWYPGYNTP(1)
HSWFWQAWPPQL(1)
HIRLPTWWGAYP(1)
FHENWPSGGGSA(1)
FHKNWPIWWYPP(1)
WHNPYQLWSWRW(1)
ASQVGPAHTSTV(1)
SDRIPSLRAHTV(1)
ITKSGLTHLYPV(1)
GPQVLANIPHFP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22606046</Reference>
<Target_Name>72 kDa type IV collagenase</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 authors showed that M204C4 (HWWQWPSSLQLRGGGS) and M205C4 (HNWTRWLLHPDRGGGS) inhibited the activity of MMP-2 in a dose dependent manner in vitro. Two peptides reduced MMP-2 mediated invasion of the pancreatic cancer cell lines PANC-1 and CFPAC-1, but not affected the expression and release of MMP-2. Furthermore, these two peptides could suppress tumor growth in vivo.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1970</BiopanningDataSetID>
<Peptides>CTATSHLFC(4)
CGNSWYNSC(3)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22653674</Reference>
<Target_Name>IgGs purified from equine sera</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>Phages library were added to the microtiter well adsorbed with negative IgG firstly.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1971</BiopanningDataSetID>
<Peptides>TTSVLLHCIEWTILNQ</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:22683611</Reference>
<Target_Name>Caspase-6, CASP-6</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>Linear-lib M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In each round, biotinylated zymogen caspase-6 was incubated with the amplified phage from previous round and the caspase-6-phage complex was captured by NeutrAvidin-coated plate that has been previously blocked by block buffer.</Brief_Description>
<BiopanningDataSet_Comments>After four rounds of binding selection, individual phage clones were analyzed in a high-throughput phage spot ELISA using plate-immobilized zymogen caspase-6 as the target. The binding signal of the same phage particle to NeutrAvidin was detected as non-specific binding noise. Clones with phage-binding signal to target over 0.5 and signal/noise ratio &gt; 3 were considered to be positive clones and were subjected to DNA sequence analysis.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1972</BiopanningDataSetID>
<Peptides>VFVVCDWFDFVCALGM
VFVVCDWFEFVCTFGL
VIVSCDWVYFICELVM</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:22683611</Reference>
<Target_Name>Caspase-6, CASP-6</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>Cyclic-lib M13 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In each round, biotinylated zymogen caspase-6 was incubated with the amplified phage from previous round and the caspase-6-phage complex was captured by NeutrAvidin-coated plate that has been previously blocked by block buffer.</Brief_Description>
<BiopanningDataSet_Comments>After four rounds of binding selection, individual phage clones were analyzed in a high-throughput phage spot ELISA using plate-immobilized zymogen caspase-6 as the target. The binding signal of the same phage particle to NeutrAvidin was detected as non-specific binding noise. Clones with phage-binding signal to target over 0.5 and signal/noise ratio &gt; 3 were considered to be positive clones and were subjected to DNA sequence analysis.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1973</BiopanningDataSetID>
<Peptides>FLSPAQRFELFP(4)
WPSAAEAFSKSP(3)
APSAADQFMALF(2)
MPSAVHLFETMR(1)
DNSAAQYFSRMP(1)
NSAAYSFTLFPG(1)
QSAASLFNNSMN(1)
SAADRFRTGPMP(1)
SAADRFSRYHER(1)
GASAAENFLKSL(1)
DSAASHFTTQFR(1)
KSAAEQFSLTMA(1)
SAANKFTVATMP(1)
GASAVTRFQSMY(2)
SAADHWRLSALI(1)
YQSAASKWSTYY(1)
SAASKWHNALAQ(1)
SAVHQWATQFLM(1)
SAVNNWESFYGW(1)
SHTAAHHFQVML(1)
SMTAATVFWTQM(1)
YNTAATKFSLQL(1)
STAVQQFQNTLS(1)
VSTAVSRFEALT(1)
AEPAAARWQASL(1)
QPAAVRLFEMMT(1)
EPNIADFFYRSM(1)
ADQNSFISALFQ(1)
TQNMHKFFEQES(1)
AKITRTLSLPFS(2)
QKITTTFFSPLM(1)
AKLTSTFSESPH(1)
SKLTSTLTQLAS(1)
AHPITQHDTSAR(1)
SPLLDLLKLRSP(1)
SPQQQTLATFFG(1)
APIQDNTLGRWF(1)
TFPQNVPLPILP(1)
EHEQHLSLQRWF(1)
EELFTRNVLNWP(1)
SIAEKWTTYLRK(1)
KSLSRHDHIHHH(22)
KSVSSQDHIHHQ(1)
RMNSPLDVLHHR(1)
SSLHTHQTPMFM(1)</Peptides>
<Motif>P-S-A-[AV]-X-R-[FW]-[ES]-L-S-P, A-K-[IL]-[TQ]-X-T-L-X-L, K-S-L-S-R-X-D-X-I</Motif>
<Unique_Sequence_Number>45</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22716192</Reference>
<Target_Name>Anti-MgPa polyclonal antibody</Target_Name>
<Template_Name>Adhesin P1</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 each round, the phage eluates were added into the microtiter plate coated with normal rabbit antiserum at room temperature and incubated for 1 h. The preincubation procedures were performed 5 times to remove those phages that possibly nonspecifically bind to rabbit antiserum.</Brief_Description>
<BiopanningDataSet_Comments>Results of bioinformatics analysis by MIMOX demonstrated that the key consensus amino acid residues in the aligned mimotopes may be S, A, and F for cluster 1; A, K, I, T, and L for cluster 2; and K, S, L, R, D, and I for cluster 3. Three representative phages could recognize sera from M. genitalium-positive patients to varying degrees, whereas they could not recognize the sera from Mycoplasma pneumoniae-positive patients or the sera from healthy people. These findings will help to clarify the mimic epitopes of MgPa to facilitate diagnosis of the antigen and to understand the antigenic structure of MgPa.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1974</BiopanningDataSetID>
<Peptides>WDSDCKRSCRVH(1)
LTWVSDSKSGNT(1)
TIAPSWATDSKP(1)
TPNNAQKQPQLP(1)
SWMPDSKVFASH(1)
WETDQKFKQRVA(2)
SAYDDVKRFYTN(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:22720103</Reference>
<Target_Name>Anti-VSG LiTat 1.3 polyclonal antibody</Target_Name>
<Template_Name>Variant surface glycoproteins LiTat 1.3, VSG LiTat 1.3</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>A negative selection was conducted with endemic negative serum antibodies coated on magnetic particles.</Brief_Description>
<BiopanningDataSet_Comments>Eight of 188 phage clones reacted in the sandwich ELISA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1975</BiopanningDataSetID>
<Peptides>ETDNMKPLHLRQ(1)
VNDASKLFYPRS(1)
WPTSWHMWLANR(1)
GVPDNHKPARTQ(1)
ALPTHMNWVMPV(1)
TWPQWWWTNSKG(1)
NPPIWGTATKGI(1)
FWKPHRTHFWWG(1)
YNWETDKPMPVP(1)
TWWWHSLAKTPH(1)
TTWNFKHWWPYR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22720103</Reference>
<Target_Name>Anti-VSG LiTat 1.3 polyclonal antibody</Target_Name>
<Template_Name>Variant surface glycoproteins LiTat 1.3, VSG LiTat 1.3</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>A negative selection was conducted with endemic negative serum antibodies coated on magnetic particles.</Brief_Description>
<BiopanningDataSet_Comments>Eleven of 188 phage clones reacted in the sandwich ELISA.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>