<result><BiopanningDataSet><Item><BiopanningDataSetID>1926</BiopanningDataSetID>
<Peptides>TGLESGHGPGDS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22236882</Reference>
<Target_Name>Purified immunoglobulin G (IgG) from sera of knee OA patients</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>To increase the screening specificity, microtiter wells were coated with purified sera IgG from healthy controls to absorb non-specific phages from the phage random peptide library, and the unbounded phages were then incubated with sera IgG from knee OA patients to screen for phages containing knee OA-specific peptides.</Brief_Description>
<BiopanningDataSet_Comments>The phage clone with inserted peptide TGLESGHGPGDS (named KOA1) showed 90% positive reaction rate with the knee OA patients, significantly higher than that with the knee RA patients (27.8%), the nonerosive hand OA patients (34.3%), the erosive hand OA patients (31.3%) and the healthy controls (12.0%), but not the hip OA patients (82.5%). The novel knee OA mimic peptide KOA1 could be a potential serum biomarker for knee OA.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1927</BiopanningDataSetID>
<Peptides>NHWSDKRAQITI(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:22239472</Reference>
<Target_Name>Gadolinium  oxide  (GdO)</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>These peptide adhesion domains are exploited to effectively decorate GdO particles with fluorescently labeled poly(ethylene oxide) (PEO), proving to result in a stable surface modification as shown by significant reduction of protein adsorption by 80%, compared to nonfunctionalized particles.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1928</BiopanningDataSetID>
<Peptides>CHMRNTIHC(1)
CHSSLLNPC(1)
CNSKLHAFC(1)
CYNPRLHIC(1)
CMEPKSRYC(1)
CSNRMATTC(1)</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:22249604</Reference>
<Target_Name>Anti-gp75 monoclonal antibody 5E7C</Target_Name>
<Template_Name>P. brasiliensis 75-kDa 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>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The interaction between the selected phage clones and the 5E7C mAb was evaluated by in vitro binding assays. Binding assay showed that phage displaying P13 (CHSSLLNPC) is a putative mimotope to anti gp75 mAb.</Affinity_Measurement_Description>
<Brief_Description>Library was cleaned with mAb 17C (anti-gp43) that belongs to the same isotype of the mAb 5E7C (IgG2a) to eliminate non-specific phage clones to the target molecule (mAb 5E7C).</Brief_Description>
<BiopanningDataSet_Comments>Aiming to improve the antigenic potential of the peptide selected sequence, five amino acids similar to the phosphatase sequence showing greater homology were added to the N-terminal and C-terminal, flanking the initial sequence of nine amino acids. That approach led to a synthetic peptide (NANEAHSSLLNNALSI) named P2, which was synthesized and tested against PCM patients' sera to check whether it was recognized. There was significant recognition of P2 by sera of untreated PCM patients when compared with normal human sera. Sera from treated PCM group, patients with other mycosis or co-infected with HIV had much lower recognition of P2 than untreated patient group. The test showed a sensitivity of 100 and 94.59% of specificity in relation to human sera control. These data indicate a potential use of P2 as diagnostic tool in PCM. Its application for serological diagnosis of PCM may contribute to the development and standardization of simpler, faster and highly reproducible immunodiagnostic tests at low cost.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1929</BiopanningDataSetID>
<Peptides>DSGLCMPRLRGCDPR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:22257077</Reference>
<Target_Name>Low-density lipoprotein receptor</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>Not determined.</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>From an initial phage display biopanning, a series of peptide ligands for the LDLR was optimized leading to size reduction and improved receptor binding affinity with the identification of peptide 22 and its analogues. Further real-time biphoton microscopy experiments on living mice demonstrated the ability of peptide 22 to efficiently and quickly cross CNS physiological barriers. This validation of peptide 22 led us to explore its binding on the extracellular LDLR domain from an NMR-oriented structural study and docking experiments.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1930</BiopanningDataSetID>
<Peptides>WFHCPYDLCHIL
QWECPYGLCWIQ</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:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>TN6 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1931</BiopanningDataSetID>
<Peptides>RSCNYYGTCLH
HDCQYYGTCLH
FACHYYGTCLH
RPCDYYGTCFD</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>TN7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1932</BiopanningDataSetID>
<Peptides>LPCDYYGTCLD
LPCSYYGTCLH
LSCDYYGTCLR
LACHYYGTCLH
RPCNYYGTCLH
DPCSYYGTCLH
FACHYYGTCLH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22263840</Reference>
<Target_Name>Fibrin</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>TN7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1933</BiopanningDataSetID>
<Peptides>RFCNPFAWLCFD
HFCSPFHLHCFR
HFCNPFFFPCLH
HFCSPFLLDCPH
RFCNPFLLDCAH
HFCFWPIGNCPH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22263840</Reference>
<Target_Name>Fibrin</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>TN8 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1934</BiopanningDataSetID>
<Peptides>DCDDHWPRWCH
FCRHFNFSFCF</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:22263840</Reference>
<Target_Name>Fibrin</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>TN9 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1935</BiopanningDataSetID>
<Peptides>NHGCYNSYGVPYCDYS</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:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>TN10 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1936</BiopanningDataSetID>
<Peptides>GPRPLSNSVSAI
GPRPNSPAPAGS</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:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1937</BiopanningDataSetID>
<Peptides>GPRPTSS
GPRPTYM
GPRPPMV
GPRPPTD
GPRPPYA
GPRPPTI
GPRPPDW</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1938</BiopanningDataSetID>
<Peptides>CHPMAPKYC
CHPMAPRYC
CHPQAGASC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22263840</Reference>
<Target_Name>Soluble fibrin fragment DD(E)</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>Before each round, libraries were depleted of fibrinogen binders by incubating the phage with biotinylated fibrinogen bound to bead immobilized streptavidin.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1939</BiopanningDataSetID>
<Peptides>HWGNHSKSHPQR(20)
KSLSRHDHIHHH(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22265946</Reference>
<Target_Name>Anti-RPV-H monoclonal antibody C1</Target_Name>
<Template_Name>Hemagglutinin glycoprotein</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>Four independent peptide library screenings yielded 80 fourth-round phage clones that were selected by the C1 mAb. In twenty phage clones the amino acid sequence HWGNHSKSHPQR (Domain 1 (D1)) was obtained, whilst five phage clones had the amino acid sequence KSLSRHDHIHHH (D2). The alignment analysis with the RPV RBOK H protein revealed that residues within D1 aligned to amino acids 309-320 in H, whereas residues within D2 aligned to amino acids 529-540.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1940</BiopanningDataSetID>
<Peptides>YQVTQSKVMSHR[0.479 ± 0.079]
YQVTPIKLISHI[0.526 ± 0.046]
NHVTAIKLITHI[0.521 ± 0.048]
YQVTQSKEISHR[0.706 ± 0.038]
YHVTPIKLISHI[0.613 ± 0.056]</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:22314514</Reference>
<Target_Name>Phosphocarrier protein HPr</Target_Name>
<Template_Name>Phosphoenolpyruvate-protein phosphotransferase</Template_Name>
<Structure_of_Target_Template_Complex>2XDF,3EZA,3EZB,3EZE,</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 of selected clones to phosphocarrier protein HPr was confirmed by ELISA. The experiments were performed triplicate. Absorbance at 410 nm was determined, reproduced from the graph and expressed as the mean ± SD. The original library was served as the control (with A410 of 0.214 ± 0.040).</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The single-stranded DNAs of the 20 selected phages were isolated, sequenced, and five corresponding peptides were synthesized. Only one of the five peptides, AP1 (YQVTQSKVMSHR) was found to inhibit the growth of Escherichia coli cells efficiently (IC50~50 μM). Molecular modeling reveals that AP1 may block the EI-HPr interaction and phosphotransfer. Interestingly, AP1 was also found to induce cell aggregation in a concentration-dependent manner.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1941</BiopanningDataSetID>
<Peptides>EPLQLKM(3)
STAPRPY(3)
SPPQSRA(3)
TTPTKSA(2)
SPLSEHS(2)
IPTLPSS(1)
HWGMWSY(1)
QPLQLQV(1)
SPLQMMQ(1)
LTIPTTA(1)
VVGTANT(1)
MYASSSK(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:22322196</Reference>
<Target_Name>Human bone marrow-derived mesenchymal stem cell, hBMMSCs</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 negative selection procedure, the library was incubated with the synovial cells for 1 h to exclude the synovial cell affinity phage clones.</Brief_Description>
<BiopanningDataSet_Comments>The authors identified an MSC-homing peptide EPLQLKM (E7) through phage display and constructed an MSC-homing device by conjugating E7 with PCL electrospun meshes. The E7-conjugated PCL electrospun meshes have shown an apparent MSC-homing property in vivo. In addition, the E7-conjugated PCL electrospun meshes have shown specificity toward MSCs compared with the RGD-conjugated PCL electrospun meshes. The current study offers a promising way to improve MSC-based TE repair.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1942</BiopanningDataSetID>
<Peptides>EPLQLKM(7)
IPTLPSS(6)
MYASSSK(2)
QPWPTSI(2)
SPPQSRA(1)
HWGMWSY(1)</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:22322196</Reference>
<Target_Name>Human bone marrow-derived mesenchymal stem cell, hBMMSCs</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 negative selection procedure, the library was incubated with the synovial cells for 1 h to exclude the synovial cell affinity phage clones.</Brief_Description>
<BiopanningDataSet_Comments>The authors identified an MSC-homing peptide EPLQLKM (E7) through phage display and constructed an MSC-homing device by conjugating E7 with PCL electrospun meshes. The E7-conjugated PCL electrospun meshes have shown an apparent MSC-homing property in vivo. In addition, the E7-conjugated PCL electrospun meshes have shown specificity toward MSCs compared with the RGD-conjugated PCL electrospun meshes. The current study offers a promising way to improve MSC-based TE repair.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1943</BiopanningDataSetID>
<Peptides>EPLQLKM(10)
IPTLPSS(4)
HWGMWSY(3)
LTIPTTA(2)
MYASSSK(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:22322196</Reference>
<Target_Name>Human bone marrow-derived mesenchymal stem cell, hBMMSCs</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 negative selection procedure, the library was incubated with the synovial cells for 1 h to exclude the synovial cell affinity phage clones.</Brief_Description>
<BiopanningDataSet_Comments>The authors identified an MSC-homing peptide EPLQLKM (E7) through phage display and constructed an MSC-homing device by conjugating E7 with PCL electrospun meshes. The E7-conjugated PCL electrospun meshes have shown an apparent MSC-homing property in vivo. In addition, the E7-conjugated PCL electrospun meshes have shown specificity toward MSCs compared with the RGD-conjugated PCL electrospun meshes. The current study offers a promising way to improve MSC-based TE repair.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1944</BiopanningDataSetID>
<Peptides>FHWTWQFPYTST(3)
FHWNYYLYSQVS(3)
WHWQWWLQTDAT(2)
FHWWPPSLANQP(1)
WHWNAWNWSSQQ(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:22322353</Reference>
<Target_Name>Whole Mycobacterium bovis cells, WCA</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>1945</BiopanningDataSetID>
<Peptides>SEFPRSWDMETN(7)
FEFPRSWDMETN(1)
NFRVSIDVVKSR(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:22322353</Reference>
<Target_Name>Ethanol-extracted Mycobacterium bovis cell surface antigens, EEA</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>1946</BiopanningDataSetID>
<Peptides>GNLLHNHETYRH(2)
HSLRWDWTARNS(1)
HSLRDDIRTMTA(1)
HKWGGNTLMAFR(1)
HKPPTHIYLSWR(1)
KVWPNMFANENI(1)
KLWSIPKDLGPP(1)
GYVHRELAWNMN(1)
NMELHPHSLPRP(1)</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:22322353</Reference>
<Target_Name>Cell surface lipoprotein MPB83</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>1947</BiopanningDataSetID>
<Peptides>QEINSSY[0.65 ± 0.02]
SHPRLSA[0.72 ± 0.05]
SMPNPMV[0.69]
GLQQVLL[0.79 ± 0.04]
HELSVLL[0.63 ± 0.04]
YAPQRLP[0.58]
TPRTLPT[0.51 ± 0.03]
APVHSSI[0.45 ± 0.02]
APPHALS[0.59]
TFSNRFI[0.40 ± 0.02]
VVPTPPY[0.76 ± 0.06]
ELAPDSP[0.59]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22363498</Reference>
<Target_Name>Anti-LPS monoclonal antibody</Target_Name>
<Template_Name>Lipopolysaccharide, LPS</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>In phage ELISA, absorbance was measured at 490 nm. Each experiment was repeated three times. Data were reproduced from the graph and expressed as means ± SD. Phage 2Ab as negative control showed no ELISA signal.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The data demonstrate the identification of synthetic peptides that mimic LPS by interacting with TLR-4. This LPS mimotope-TLR-4 interaction will allow for the development and use of these peptides as a new class of adjuvants, namely TLR-4 agonists.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1948</BiopanningDataSetID>
<Peptides>TLHLHHL(15)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:22372912</Reference>
<Target_Name>Transcriptional regulatory protein devR (dosR)</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 first round, the phage library was incubated with (His)6-DevR immobilized on Ni2+ NTA (nitrilotriacetic acid) magnetic agarose beads. The loosely bound phages were discarded by elution with DevR D54N mutant protein (100μg/mL concentration), which differs from the wild-type protein at the phosphorylation site. A second elution was performed with buffer containing 250 mM imidazole that released the His6-tagged protein along with the tightly bound phages. Three rounds of panning were performed using the twin elutions approach, and each time the phages in the imidazole elution were amplified and used as an input for the next round of panning. The fourth and fifth rounds were performed on plate to eliminate bead binders. The loosely bound phages were\r\nfirst eluted with mutant D54N DevR protein and then with 0.2 M glycine, pH 2.2. In the fifth (final) round of panning, a penultimate elution using phosphorylated DevS was carried out prior to final elution of the bound phages using 0.2 M glycine.</Brief_Description>
<BiopanningDataSet_Comments>DevRS1 (TLHLHHL) inhibited DevR-regulated transcription and survival of nonreplicating tubercle bacilli in a hypoxia model of dormancy. DevRS1 peptide-mediated inhibition demonstrates the efficacy of intercepting DevR function to block hypoxic adaptation of M. tb.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1949</BiopanningDataSetID>
<Peptides>HTPPVTS(5)
ASTLPKA(3)
QPQVPDA(3)
ALTPTPP(2)
ILGVGLP(2)
SILPYPY(2)
LGSTTPP(1)
SPIWMHS(1)
SPLLSTP(1)
AXQISPP(1)
TAPTSPS(1)
QPLELPN(1)
AAQTSTP(1)
FSAHAHL(1)
NQDVPLF(1)
TPRLLVE(1)
HAIYPRH(1)
IPTLPSS(1)
EATTRAY(1)
YSIPKSS(1)
ATPLWLK(1)
FPPNKES(1)
LPSYHVP(1)
YRAPWPP(1)
DTWRPVR(1)
THPLLLS(1)
SPQMTLS(1)
SSHTISF(1)
HPFEHFS(1)
STATSKT(1)
MLQPQAP(1)
WGGLPEP(1)
EPLVQHP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>33</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:22404231</Reference>
<Target_Name>Thiamethoxam, TMX</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>One hundred microliters of the diluted phage library was then introduced into the TMX suspension and incubated for 1 h with gentle rocking. The sample was washed several times with TMX-saturated 0.1% TBST buffer and transferred to new centrifuge tubes. This step removed nonspecific binding phage or any phage with a strong affinity to the polypropylene centrifuge tubes.</Brief_Description>
<BiopanningDataSet_Comments>The six most strongly binding phages exhibit at least 1000 times the binding affinity of wild-type M13 and express heptapeptide sequences that are rich in hydrophobic, hydrogen-bonding amino acids and proline. Among the peptide sequences identified, M13 displaying the pIII domain heptapeptide ASTLPKA exhibits the strongest binding to thiamethoxam in competitive binding assays. Electron and confocal microscopy confirm the specific binding affinity of ASTLPKA to thiamethoxam.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>1950</BiopanningDataSetID>
<Peptides>FPMFNHWEQWPP(3)</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:22421431</Reference>
<Target_Name>Epidermal growth factor receptor</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>After the fourth round of panning, seven phage clones from the 12-mer peptide displayed phage library were randomly selected and used for ELISA to rhEGFR. Three of the seven clones from the 12-mer peptide library showed a specific affinity to rhEGFR, and all three encoded the same 12 amino acid peptide sequence, FPMFNHWEQWPP.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>