<result><BiopanningDataSet><Item><BiopanningDataSetID>3176</BiopanningDataSetID>
<Peptides>WPTDHQMLRIPM(342)
QSDPWLVSRWFA(66)
TYPSTQWFFAKF(60)
TLPPEAWWRTMY(52)
SFPDVQWWRNQY(50)
YPSSEQLLAWWG(40)
ELPSVEQLWDFF(37)
WPWDPLRISDWL(36)
TWVSDLDMWLGA(28)
RLPTSMELLAAF(24)
SDSWVRGLNYWY(16)
SYWVPDIVWAGL(15)
QDPWKVKNWINQ(15)
GLPSSAELERLW(14)
LPWPSDQIILMW(14)
FFPSEQVLIAAL(12)
LPSSAELLWALR(9)
WDPWQIDRWVLL(8)
FDPLNIRHWIWG(7)
DPWFINEWIRIP(4)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method></Experimental_Method>
<Rounds_of_Panning>0</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>Not determined.</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>The Ph.D. library was amplified once with no selection and used as the unselected library control (replicate 2).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3177</BiopanningDataSetID>
<Peptides>DWSSWVYRDPQT(3030)
WPLWSFDWPQNA(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method></Experimental_Method>
<Rounds_of_Panning>0</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>Not determined.</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>The Ph.D. library was amplified four times with no selection and used as the unselected library control (replicate 1).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3178</BiopanningDataSetID>
<Peptides>WPTDHQMLRIPM(40.15%)
QSDPWLVSRWFA(8.55%)
DWSSWVYRDPQT(7.82%)
TYPSTQWFFAKF(1.90%)
ELPSVEQLWDFF(1.87%)
YPSSEQLLAWWG(1.74%)
WPSDNQLLQIHV(1.64%)
RLPTSMELLAAF(1.64%)
TWVSDLDMWLGA(1.53%)
WDPWQIDRWVLL(1.47%)
NAPSIYDWLATL(1.20%)
KLPSPYDLYLFL(1.15%)
TLPPEAWWRTMY(0.72%)
WPWDPLRISDWL(0.62%)
QDPWKVKNWINQ(0.56%)
FFPSEQVLIAAL(0.43%)
SWDPLLVSAWIK(0.43%)
WPLWSFDWPQNA(0.38%)
WLTEDMSAFMSY(0.34%)
DPWFINEWIRIP(0.32%)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>IL-4-polarized M2 macrophage</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>Subtractive phage display using murine IL-4- polarized M2 (&quot;anti-inflammatory&quot;) macrophage for positive selection and IFN-γ- and LPS-polarized M1 (&quot;pro-inflammatory&quot;) macrophage for negative selection was completed in biological duplicates with one initial enrichment selection followed by three rounds of paired negative/positive selection.</Brief_Description>
<BiopanningDataSet_Comments>Barcoded phage library amplicons were sequenced by Illumina, and the top 20 most abundant sequences from the last rounds are shown （replicate 1).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3179</BiopanningDataSetID>
<Peptides>WPTDHQMLRIPM(32.14%)
TYPSTQWFFAKF(9.51%)
SFPDVQWWRNQY(5.16%)
WPWDPLRISDWL(5.08%)
TLPPEAWWRTMY(4.42%)
QSDPWLVSRWFA(3.59%)
YPSSEQLLAWWG(3.52%)
RLPTSMELLAAF(3.21%)
GLPSSAELERLW(2.47%)
ELPSVEQLWDFF(2.44%)
TWVSDLDMWLGA(1.89%)
QDPWKVKNWINQ(1.78%)
FFPSEQVLIAAL(1.64%)
SDSWVRGLNYWY(1.27%)
FDPLNIRHWIWG(1.20%)
WDPWQIDRWVLL(1.19%)
LPWPSDQIILMW(1.17%)
DPWFINEWIRIP(0.88%)
LPSSAELLWALR(0.81%)
SYWVPDIVWAGL(0.74%)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>IL-4-polarized M2 macrophage</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>Subtractive phage display using murine IL-4- polarized M2 (&quot;anti-inflammatory&quot;) macrophage for positive selection and IFN-γ- and LPS-polarized M1 (&quot;pro-inflammatory&quot;) macrophage for negative selection was completed in biological duplicates with one initial enrichment selection followed by three rounds of paired negative/positive selection.</Brief_Description>
<BiopanningDataSet_Comments>Barcoded phage library amplicons were sequenced by Illumina, and the top 20 most abundant sequences from the last rounds are shown (replicate 2).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3180</BiopanningDataSetID>
<Peptides>SCNVAGGTCGLT
YPSSEQLLAWWG
VAGPQITKYNVP
ESSPATKFVRPS
VCLYVNIECSQQ
LGPQRQENSHPF
GLPIWPQHLTNT
RMDPDQPRARVA
GFGGLVDDVRGG
INIPDEQSSNHL
QSDPWLVSRWFA
ALVNQADGDSTQ
SLYGKKSPMGYP
YSDEGTPRSGGL
WPTDHQMLRIPM</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>15</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>IL-4-polarized M2 macrophage</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>Subtractive phage display using murine IL-4- polarized M2 (&quot;anti-inflammatory&quot;) macrophage for positive selection and IFN-γ- and LPS-polarized M1 (&quot;pro-inflammatory&quot;) macrophage for negative selection was completed in biological duplicates with one initial enrichment selection followed by three rounds of paired negative/positive selection.</Brief_Description>
<BiopanningDataSet_Comments>From the last round of each duplicate phage display experiment, 20 phage plaques were randomly selected for Sanger sequencing (replicate 1).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3181</BiopanningDataSetID>
<Peptides>WPTDHQMLRIPM
ELPSVEQLWDFF
WPTDHQMLRIPM
TLPPEAWWRTMY
MLPSPELLWEWL
WDPWQIDRWVLL
GLPSSAELERLW
TYPSTQWFFAKF
FFPSEQVLIAAL
GLPSSAELERLW
QDPWKVKNWINQ
WPTDHQMLRIPM
GLPSSAELERLW
WPWDPLRISDWL
WDPWQIDRWVLL
TYPSTQWFFAKF
ELPSVEQLWDFF
YPSDLDILRLFS
GLPSSAELERLW
SDSWVRGLNYWY</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:26161996</Reference>
<Target_Name>IL-4-polarized M2 macrophage</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>Subtractive phage display using murine IL-4- polarized M2 (&quot;anti-inflammatory&quot;) macrophage for positive selection and IFN-γ- and LPS-polarized M1 (&quot;pro-inflammatory&quot;) macrophage for negative selection was completed in biological duplicates with one initial enrichment selection followed by three rounds of paired negative/positive selection.</Brief_Description>
<BiopanningDataSet_Comments>From the last round of each duplicate phage display experiment, 20 phage plaques were randomly selected for Sanger sequencing (replicate 2).</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3182</BiopanningDataSetID>
<Peptides>CPLHARLPC(82.49%)[2.16693±0.28562]
CFDTRSLVC(5.05%)[1.46493±0.08252]
CDHGYLPSC(0.92%)[0.72612±0.07109]
CHYDGARAC(0.81%)[1.04729±0.07235]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:24265677</Reference>
<Target_Name>Mycobacterium tuberculosis △leucineD and △panthothenateCD double auxotroph, △leu/△pan</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>Microtiter plate wells were coated with 100 ml of mycobacteria suspension, with an optical density of 1.0 at 660 nm in carbonate buffer, and incubated overnight at 4uC. Absorbance was determined using a microtiter plate reader at the wavelength of 405 nm.</Affinity_Measurement_Description>
<Brief_Description>Five rounds of biopanning were performed. The first three rounds were targeted against M. tb (△leu/△pan), followed by a subtraction round against M. smegmatis. The fifth round of positive selection was against the targeted M. tb (△leu/△pan).</Brief_Description>
<BiopanningDataSet_Comments>We further showed that the clone displaying the CPLHARLPC peptide which was identified by Illumina sequencing as the most enriched, binds better to mycobacteria than three clones selected by random picking. Using surface plasmon resonance, we showed that chemically synthesised CPLHARLPC peptide binds to a 15 KDa peptide from M.tb H37Rv whole cell lysates.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3183</BiopanningDataSetID>
<Peptides>QCVPLKCLWDRCE(110)
TCLCKRCIKELCC(36)
VCERQVCYLMSCW(22)
YCVWDKCLWLMCE(16)
ACDARPCPQTYCL(12)
ACGMSICVLYGCN(9)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Human beta-FXIIa</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>XCX4CX4CX phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Identical peptides would be considered as target-specific peptides. We repeated a first round of selection against FXIIa and found that only six peptide sequences were common in both pools. Four of them, QCVPLKCLWDRCE, ACDARPCPQTYCL, TCLCKRCIKELCC and YCVWDKCLWLMCE, corresponded to confirmed binding motifs that were previously found after three rounds of selection.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3184</BiopanningDataSetID>
<Peptides>ACKRTHCLPPCCGGSG(743)
ACPLLPPCADDCGGSG(701)
ACSRHCLTLPPCGGSG(364)
ACPLLPPCSLDCGGSG(317)
ACRQLPPCSFECGGSG(302)
ACSWRCPSLPPCGGSG(194)
ACSVLPPCSFSCGGSG(148)
ACNTLCPYLPPCGGSG(146)
ACYQLPPCDHSCGGSG(140)
ACPILPPCHAHCGGSG(135)
ACHLPPCSLHLCGGSG(125)</Peptides>
<Motif>LPP</Motif>
<Unique_Sequence_Number>6243</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Sortase A from S. aureus (SrtA)</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>CX3CX4CG, CX4CX3CG, CX4CX4CG, CX3CX5CG and CX5CX3CG phage display library pool</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>3185</BiopanningDataSetID>
<Peptides>MAACSILPPCNPPQCGGSG(5860)
MAACPLLPPCHLPQCGGSG(4327)
MAACTLLPPCTPDQCGGSG(3990)
MAACPELPPCQLMLCGGSG(2326)
MAACQVLPPCGLQLCGGSG(2302)
MAACRPKQCWQLPPCGGSG(1798)
MAACSFIQDCHPQSCGGSG(1574)
MAACPMLPPCDLSYCGGSG(1258)
MAACRQLPPCAEYVCGGSG(1231)
MAACLPPHSCWNQVCGGSG(1227)
MAACPSLPPCWQLQCGGSG(1131)</Peptides>
<Motif>LPP</Motif>
<Unique_Sequence_Number>2776</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Sortase A from S. aureus (SrtA)</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>CX3CX6CG, CX6CX3CG, CX4CX5CG and CX5CX4CG phage display library pool</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>3186</BiopanningDataSetID>
<Peptides>MAACTQSACSARVVCGGSG(5410)
MAACAPDQCTKFTMCGGSG(2493)
MAACTYALCTARTFCGGSG(1905)
MAACSASQCSARIGCGGSG(1493)
MAACMLSGSCTARSCGGSG(1381)
MAACKHSDCTARFPCGGSG(1315)
MAACFRYQCTARSHCGGSG(1081)
MAACPVKPSCHSGRCGGSG(1056)
MAACPLSACSGRTLCGGSG(1026)
MAACAYRSCQGTARCGGSG(918)
MAACWTPTCSARSHCGGSG(890)</Peptides>
<Motif>[TS]-A-R, [KR]-[FY]-[ST]-L</Motif>
<Unique_Sequence_Number>6906</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Urokinase-type plasminogen activator</Target_Name>
<Template_Name>Urokinase plasminogen activator surface receptor</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>CX3CX6CG, CX6CX3CG, CX4CX5CG and CX5CX4CG phage display library pool</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>3187</BiopanningDataSetID>
<Peptides>HCWVSACRHWRCQSHS(795)
ACESLTCALIVCQSHS(434)
VCLRQTCSSANCGSHS(425)
VCDQWACGQEWCVSHS(381)
RCTGRSCEWHACGSHS(369)
QCWQMPCSLGSCPSHS(344)
WCWYIGCAGIGCASHS(322)
KCSDQPCELMACKSHS(319)
ACDARPCPQTYCLSHS(307)
SCISRKCLAMQCHSHS(300)
GCGAVACCLRSCQSHS(300)</Peptides>
<Motif>RPCP, VXXKCL</Motif>
<Unique_Sequence_Number>17469</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Human beta-FXIIa</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>XCX4CX4CX phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3188</BiopanningDataSetID>
<Peptides>MADCWDSVCYRVLCWSHS(704)
MADCYQLCRVSCESHS(501)
MAMCEQRACTFRECWSHS(417)
MARCFIYCRTLCMSHS(415)
MANCFQTCRVSCYSHS(350)
MAGCFTPCRTMCWSHS(317)
MAWCATDLCDACVCQSHS(309)
MATCSWGKCQVTDCGSHS(295)
MAQCWIACRVVCLSHS(292)
MAWCHTSCQVACSSHS(290)
MARCLGHRCGAWICSSHS(287)</Peptides>
<Motif>[FYW]-X-X-C-R-V</Motif>
<Unique_Sequence_Number>3532</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Plasma kallikrein (EC:3.4.21.34)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>XCX3CX3CX and XCX4CX4CX phage display library pool</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>3189</BiopanningDataSetID>
<Peptides>MAECISSVCTRGVCLSHS(1791)
MATLSGALH*AVYFSL(1248)
MAKCWRGDCALSVCASHS(1064)
MASCCACVGFVCLTP(808)
MASCEACLCMGLCVLLTP(804)
MAHCAYLRCTLLLCQSHS(798)
MASCRDVCCSHCLSHS(795)
MAGCPEAACCLQVCGSHS(754)
MAYCTLGCDTDCSSHS(718)
MATCRQGCVGACSSHS(718)
MAQCQTRCTAVCASHS(702)</Peptides>
<Motif>HPQ</Motif>
<Unique_Sequence_Number>498</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:25348396</Reference>
<Target_Name>Streptavidin</Target_Name>
<Template_Name>Biotin</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>XCX3CX3CX and XCX4CX4CX phage display library pool</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>3190</BiopanningDataSetID>
<Peptides>RVRSAPSSS(17)[2.014 ± 0.067]
RVRSYSPHL(6)[NT]
RVRSNAASM(3)[NT]
RVRSSPVVQ(1)[NT]
RVRSIPHVA(1)[NT]</Peptides>
<Motif>R-V-R-S-P-S</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:28654884</Reference>
<Target_Name>Staphylococcus aureus, S.aureus</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>pVIII-9aa phage display library (X9)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage particles bearing no recombinant insert, from superinfection of phagemid vector pC89-containing cells, served as a negative control for evaluation of   background from non-specific binding.The ability of the isolated phage clone to interact specifically with S. aureus and the efficacy of its bacteria-binding  properties were established by ELISA on a kinetic plate reader at 405 nm.</Affinity_Measurement_Description>
<Brief_Description>The library was used for pretreatment with the plastic materials which will be used to the selection protocolon-binding phage clones.</Brief_Description>
<BiopanningDataSet_Comments>A phage clone displaying peptide capable of specific binding to S. aureus cell surface, namely St.au9IVS5 (sequence peptide RVRSAPSSS) was selected from a 9-mer phage peptide library. The ability of the isolated phage clone to interact specifically with S. aureus and the  efficacy of its bacteria-binding  properties were established by using enzyme linked immune-sorbent assay  (ELISA). We also demonstrated by Western blot analysis that the most reactive and selective phage peptide binds a 78 KDa protein on the bacterial cell surface. Furthermore, we observed selectivity of phage–bacteria-binding allowing to  identify clinical isolates of S. aureus in comparison with a panel of other  bacterial species. In order to explore the possibility of realizing a selective bacteria biosensor device, based on  immobilization of affinity-selected  phage, we have studied the physisorbed phage deposition onto a mica surface. Atomic Force Microscopy (AFM) was used to determine the organization of phage on mica surface and then the binding performance of mica-physisorbed phage to bacterial target was evaluated during the time by fluorescent microscopy. The system is able to bind specifically about 50% of S. aureus cells after 15' and 90% after one hour. Due to  specificity and rapidness, this  biosensing strategy paves the way to the further development of new cheap  biosensors to be used in developing countries, as lab-on-chip (LOC) to  detect bacterial agents in clinical diagnostics applications. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3191</BiopanningDataSetID>
<Peptides>LSSTTSPRVTTS(6)[0.889 ± 0.016]
QQLPSSSTSTYP(5)[1.011 ± 0.031]
TVAHHYPPQTPL(5)[0.832 ± 0.016]
ITTGNEWSYSRK(4)[0.846 ± 0.054]
NKLPMPISVPLV(4)[0.995 ± 0.016]
TELGQVSNAIPW(3)[0.932 ± 0.021]</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:28634746</Reference>
<Target_Name>SiHa 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>The reaction was terminated by adding 2 M H2SO4 (50 ll/well) and measured at 450 nm by an ELISA reader.Irrelevant phage clone (IRP, an amplified phage clone randomly selected from the original phage-displayed peptide library) and PBS were used as negative controls. Data shown (OD450) were reproduced from Figure 1 in the reference.</Affinity_Measurement_Description>
<Brief_Description>SiHa and HEK293 cells were used as positive target cells and negative absorber cells. Phages were incubated with HEK293 cells for 1 h after which the supernatant containing unbound phages was incubated with the  blocked SiHa cells.</Brief_Description>
<BiopanningDataSet_Comments>After sequencing of positive clones, six different peptide sequences were obtained and CSP3 (QQLPSSSTSTYP) showed best affinity and specificity to SiHa cells via immunofluorescence assay. Peptide CSP3 may be a potential candidate for molecular imaging detection and targeting therapy of cervical cancer.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3192</BiopanningDataSetID>
<Peptides>SHGRITFAYFAN[3.187 ± 0.128]
KPSYNQLYQLRF[NT]
HSTLHYRFSDWP[NT]
WDTKAVTKVPSW[NT]
NIHAHETPFKMV[NT]
AEYLANPESSEA[NT]
HVVSKVLTDRTD[NT]
YMPYMPHLPQEH[NT]
WADKEHHLILRN[NT]
SDNLLIKARTSY[NT]
TPQSIGKAFQSE[NT]
LSTPNTVGLARF[NT]
FISVQNSFGIEI[NT]
KVATIRDLHSMT[NT]
TEYKKGHDPAEI[NT]
VTGLTPYISESG[NT]
HPIQSLTTNQTK[NT]
DNDENITWGLTR[NT]
AFNAHGALLFVT[NT]
KVWDFGYAFGRT[NT]
TERMSLTTRIGF[NT]
KVWSIPYAFMAR[NT]
VKVHSGQEHETW[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>23</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:28635259</Reference>
<Target_Name>Hemagglutinin, HA</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Triplicate determinations were performed at each data point, and the average OD450 nm values were determined. Data shown were reproduced from Figure 1 in the reference.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The final selected haemagglutinin-binding peptide, SHGRITFAYFAN, was conjugated to an anti-influenza A virus (IAV) antisense oligonucleotide (ODN). The delivery efficiency and the anti-IAV effects of the conjugated molecule were evaluated in a cell culture and a mouse infection model. The conjugated molecule was successfully delivered into IAV-infected host cells more efficiently than the anti-IAV ODN in vitro and in vivo. Furthermore, the conjugated molecule protected 80% of the mice from lethal challenge and inhibited the plaque count by 75%, compared to the un-conjugated molecule (60% and 40%). These findings demonstrate that the delivery of antisense oligodeoxynucleotides to infected tissues by a virus-binding peptide-mediated system is a potential therapeutic strategy against IAV.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3193</BiopanningDataSetID>
<Peptides>LYAKPRDLSSLT
HDGVSANSSIHA
STWLYPLTSLQL
IAKQTVTSSSHP
HYSDKWGHAGTE
NNPDPHYKSTWP
KAHYGFMHQLSS
MNGSPDSSQQKS
DADYTGYLDLND
GYTLQYTLPGAP
FHESWPTFLSPS
YCGGDSCLVYVD
DRTAFYSPYNLS
FHWPWWDTYVGK
MPSSSGMMIRTT
CVEFFAAVSESS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:28635259</Reference>
<Target_Name>Neuraminidase</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>Triplicate determinations were performed at each data point, and the average OD450 nm values were determined. Data shown were reproduced from Figure 1 in the reference.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3194</BiopanningDataSetID>
<Peptides>SRTGNWTRIDQS(3)
ARYFARHPTAMG(1)
DGQSDLSPRPPH(1)
FATSRLIDTLAS(1)
GSSSKGSAFVTA(1)
HTRQWSGSGQMF(1)
INPYAQHPTGSI(1)
KASFYNVTSLNE(1)
NSVHRAALGPGT(1)
NTLLLNMDPSVV(1)
RLIDKKPDAFIT(1)
SRTGIWTRTDRS(1)
WDPWSRVMGPNT(1)
WNGPKLVSNGDG(1)
YAGEPVSVPGTS(1)
YRAGQVVMNVGA(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:28482148</Reference>
<Target_Name>Eu2O3</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 high efficiency and the specificity of binding Eu2O3 nanoparticles by M13 PG-Eu-3 was further confirmed with the use of atomic force microscopic (AFM) imaging. It is easy to see that M13 PG-Eu-3 phages bind to Eu2O3 NPs with one end of the virion, where the SRTGNWTRIDQS peptide is  presented. The peptide revealed the ability to catalyze Eu2O3 nanoparticles’ formation from Eu(OH)3 and Eu(NO3)3 solutions.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3195</BiopanningDataSetID>
<Peptides>LGRFYAASG</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:28652618</Reference>
<Target_Name>Annexin A2</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>X4YX4 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Annexin A2 and a cell-internalizing, penetratin-fused version of the selected peptide (LGRFYAASG-pen) co-localized and specifically accumulated in the cytoplasm at the cell edges and cell-cell contacts. Functionally, tumor cells incubated with LGRFYAASG-pen showed disruption of filamentous actin, focal adhesions and caveolaemediated membrane trafficking, resulting in impaired cell adhesion and migration in vitro. These effects were paralleled by a decrease in the phosphorylation of both focal  adhesion kinase (Fak) and protein kinase B (Akt). Likewise, tumor cells  pretreated with LGRFYAASG-pen exhibited an impaired capacity to colonize the lungs in vivo in several mouse models.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3196</BiopanningDataSetID>
<Peptides>CNHQHQKGC(1)[108, 37.23]
CQNAHQKGC(1)[2.4, 4.18]
CQSHKNNKC(1)[N.A., N.A.]
CHDKQSKKC(1)[N.A. N.A.]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:28650615</Reference>
<Target_Name>Human Hair</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>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage enzyme-linked immunosorbent assay (ELISA) experiments were performed in order to determine the apparent binding strength (Kapp, 1.0e10 M-1) and relative affinity (RAmax) of selected phage clones in comparison to the random phage library. The first column of the affinity value is Kapp, and the second RAmax.</Affinity_Measurement_Description>
<Brief_Description>The hair samples were incubated with the shampoo formulations containing the phage library. Washing was performed using a surfactant concentration of 0.1 w/w% in each round.</Brief_Description>
<BiopanningDataSet_Comments>A peptide with the sequence of CNHQHQKGC that can bind to human hair under shampooing conditions was used to enhance the deposition of model fragrance delivery systems. These delivery systems are either based on poly(N-(2-hydroxypropyl)methacrylamide) (PHPMA) copolymers as a representative for polymeric profragrances or polyurethane/urea-type core-shell microcapsules as a model physical fragrance carrier. The incorporation of a hair binding peptide enhanced the deposition of PHPMA copolymers with a factor of 3.5-5.0 depending on the extent of peptide incorporation, whereas 10 w/w% surface functionalization of microcapsules with the peptide led to a 20-fold increase in their deposition. In a final experiment, treatment of the hair samples under realistic application conditions with the peptide-functionalized microcapsules resulted in an increase fragrance release from the hair surfaces.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3197</BiopanningDataSetID>
<Peptides>CNHQHQKGC(3)[108, 37.23]
CKSKNHPSC(1)[21.0, 18.44]
CQNAHQKGC(1)[2.4, 4.18]
CGHNKNKDC(1)[N.A., N.A.]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:28650615</Reference>
<Target_Name>Human Hair</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>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage enzyme-linked immunosorbent assay (ELISA) experiments were performed in order to determine the apparent binding strength (Kapp, 1.0e10 M-1) and relative affinity (RAmax) of selected phage clones in comparison to the random phage library. The first column of the affinity value is Kapp, and the second RAmax.</Affinity_Measurement_Description>
<Brief_Description>The hair samples were incubated with the shampoo formulations containing the phage library. Washing was performed using a surfactant concentration of 0.1 w/w% in each round.</Brief_Description>
<BiopanningDataSet_Comments>A peptide with the sequence of CNHQHQKGC that can bind to human hair under shampooing conditions was used to enhance the deposition of model fragrance delivery systems. These delivery systems are either based on poly(N-(2-hydroxypropyl)methacrylamide) (PHPMA) copolymers as a representative for polymeric profragrances or polyurethane/urea-type core-shell microcapsules as a model physical fragrance carrier. The incorporation of a hair binding peptide enhanced the deposition of PHPMA copolymers with a factor of 3.5-5.0 depending on the extent of peptide incorporation, whereas 10 w/w% surface functionalization of microcapsules with the peptide led to a 20-fold increase in their deposition. In a final experiment, treatment of the hair samples under realistic application conditions with the peptide-functionalized microcapsules resulted in an increase fragrance release from the hair surfaces.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3198</BiopanningDataSetID>
<Peptides>CNHQHQKGC(3)[108, 37.23]
CKSKNHPSC(2)[21.0, 18.44]
CQSHKNNKC(1)[N.A., N.A.]</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:28650615</Reference>
<Target_Name>Human Hair</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>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage enzyme-linked immunosorbent assay (ELISA) experiments were performed in order to determine the apparent binding strength (Kapp, 1.0e10 M-1) and relative affinity (RAmax) of selected phage clones in comparison to the random phage library. The first column of the affinity value is Kapp, and the second RAmax.</Affinity_Measurement_Description>
<Brief_Description>The hair samples were incubated with the shampoo formulations containing the phage library. The washing stringency was gradually enhanced by stepwise increasing the surfactant concentration from 0.1 w/w% (Round 1) to 0.4 w/w% (Round 4).</Brief_Description>
<BiopanningDataSet_Comments>A peptide with the sequence of CNHQHQKGC that can bind to human hair under shampooing conditions was used to enhance the deposition of model fragrance delivery systems. These delivery systems are either based on poly(N-(2-hydroxypropyl)methacrylamide) (PHPMA) copolymers as a representative for polymeric profragrances or polyurethane/urea-type core-shell microcapsules as a model physical fragrance carrier. The incorporation of a hair binding peptide enhanced the deposition of PHPMA copolymers with a factor of 3.5-5.0 depending on the extent of peptide incorporation, whereas 10 w/w% surface functionalization of microcapsules with the peptide led to a 20-fold increase in their deposition. In a final experiment, treatment of the hair samples under realistic application conditions with the peptide- functionalized microcapsules resulted in an increase fragrance release from the hair surfaces.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3199</BiopanningDataSetID>
<Peptides>CNHQHQKGC(3)[108, 37.23]
CKSKNHPSC(2)[21.0, 18.44]
CQNAHQKGC(2)[2.4, 4.18]
CGHNKNKDC(1)[N.A., N.A.]
CHDKQSKKC(1)[N.A., N.A.]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:28650615</Reference>
<Target_Name>Human Hair</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>ACX7CG phage display library</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Phage enzyme-linked immunosorbent assay (ELISA) experiments were performed in order to determine the apparent binding strength (Kapp, 1.0e10 M-1) and relative affinity (RAmax) of selected phage clones in comparison to the random phage library. The first column of the affinity value is Kapp, and the second RAmax.</Affinity_Measurement_Description>
<Brief_Description>The hair samples were incubated with the shampoo formulations containing the phage library. The washing stringency was gradually enhanced by stepwise increasing the surfactant concentration from 0.1 w/w% (Round 1) to 0.5 w/w% (Round 5).</Brief_Description>
<BiopanningDataSet_Comments>A peptide with the sequence of CNHQHQKGC that can bind to human hair under shampooing conditions was used to enhance the deposition of model fragrance delivery systems. These delivery systems are either based on poly(N-(2-hydroxypropyl)methacrylamide) (PHPMA) copolymers as a representative for polymeric profragrances or polyurethane/urea-type core-shell microcapsules as a model physical fragrance carrier. The incorporation of a hair binding peptide enhanced the deposition of PHPMA copolymers with a factor of 3.5-5.0 depending on the extent of peptide incorporation, whereas 10 w/w% surface functionalization of microcapsules with the peptide led to a 20-fold increase in their deposition. In a final experiment, treatment of the hair samples under realistic application conditions with the peptide- functionalized microcapsules resulted in an increase fragrance release from the hair surfaces.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3200</BiopanningDataSetID>
<Peptides>YPLRPNAESLRF
DPIYALSWSGMA
NATHLTADHVNK
YPSAPPQWLTNT
AQHIRSWDGFSH
LPLYTSPDKPGK
SILNYPTNPGIA
LLADTTHHRPWT
HPIRVQPDWGFL
VETHTTQWLITEV
TPMGRPHPETPA
SGKTSLISHAAL
NHLPLPPPAATM
SDTQMPPAXGRA
GYLPLHSITYRP
QLLEPVNLSTGP
WHPPKGLSPLPD
FRLPGSLINHPQ
SILSTMSPHGAT
NYNPHNPFPPAP</Peptides>
<Motif>NHT, [ST]-[IV]-L-S</Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:28453953</Reference>
<Target_Name>Human bone marrow stromal cell (hBMSC)</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>The NEB 12-mer peptide library was prescreened against sintered Hydroxyapatite (HAP) disks prior to introduction to the cells.</Brief_Description>
<BiopanningDataSet_Comments>A peptide sequence with high affinity towards apatite (VTKHLNQISQSY, VTK) was identified using phage display. In this study, a combinatorial phage display identified the cell binding sequence (DPIYALSWSGMA, DPI) which was combined with the mineral binding sequence to generate the dual peptide DPI-VTK. DPI-VTK demonstrated significantly greater binding affinity (1/KD) to apatite surfaces compared to VTK, phosphorylated VTK (VTKphos), DPIVTKphos, RGD-VTK, and peptide-free apatite surfaces (p &lt; 0.01), while significantly increasing hBMSC adhesion strength (t50, p &lt; 0.01). MSCs demonstrated significantly greater adhesion strength to DPI-VTK compared to other cell types, while attachment of MC3T3 pre-osteoblasts and murine fibroblasts was limited (p &lt; 0.01). MSCs on DPI-VTK coated surfaces also demonstrated increased spreading compared to pre-osteoblasts and fibroblasts. MSCs cultured on DPI-VTK coated apatite films exhibited significantly greater proliferation compared to controls (p &lt; 0.001). Moreover, early and late stage osteogenic differentiation markers were elevated on DPI-VTK coated apatite films compared to controls.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>