<result><BiopanningDataSet><Item><BiopanningDataSetID>3001</BiopanningDataSetID>
<Peptides>CKIMISISC(30)
CKMTRSTIC(22)
CHIPSIHSC(8)
CTHRRSTPC(5)
CPLLTKLKC(4)
CQMMLIRRC(4)
CILRKIRPC(4)
CLIRRTSIC(2)
CLHPPLTLC(2)
CLIRLILQC(2)
CMRQRRNRC(2)
CNPMTRLIC(2)
CNLLLRTQC(1)
CSRRPTSIC(1)
CRMRKTLRC(1)
CQPHHSIIC(1)
CSTHIPSHC(1)
CILRRRKRC(1)
CPRRRLKRC(1)
CHQLPIRPC(1)
CPIKTTITC(1)
CRRQTSTHC(1)
CPIRHRPIC(1)
CTLHKSRSC(1)
CTRIISNTC(1)
CKLINTLKC(1)
CQMTRSTIC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>27</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:27173134</Reference>
<Target_Name>Endothelial cells (ECs) of non-ligated right carotid artery (RCA)</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>Briefly, 1.0e11 plaque-forming units (pfu) of phages were injected intravenously into mice at 3 days after left carotid artery (LCA) ligation. After 10 minutes of circulation, the mice were anesthetized with zoletil and rompun, and pressure perfused with saline containing heparin (10 U/ml) via the left ventricle after severing the inferior vena cava to remove unbound phage. The unligated right carotid artery (RCA) was then isolated. The carotid lumen was rapidly flushed using a 29-gauge insulin syringe with 200 μL of phage elution buffer (0.2M Glycine-HCl, pH 2.2) for detachment of bound phages from endothelium and subsequently neutralized with 30 μL of 1 M Tris-HCl (pH 9.1) using a 29-gauge insulin syringe into a microfuge tube. Eluted phages from RCA were amplified in Escherichia coli ER2738 for reinjection in the next round.</Brief_Description>
<BiopanningDataSet_Comments>The peptide CLIRRTSIC selectively bound to arterial endothelial cells (ECs) exposed to disturbed flow not only in the partially ligated carotids but also in the lesser curvature and branching point of the aortic arch in mice as well as human pulmonary artery branches. Peptides were conjugated to branched polyethyleniminepolyethylene glycol polymer to generate polyplexes carrying siRNA targeting intercellular adhesion molecule-1 (siICAM-1). In mouse model, CLIRRTSIC polyplexes carrying si-ICAM-1 specifically bound to endothelium in disturbed flow regions, reducing endothelial ICAM-1 expression. Mass spectrometry analysis revealed that non-muscle myosin heavy chain II A (NMHC IIA) is a protein targeted by CLIRRTSIC peptide. Further studies showed that shear stress regulates NMHC IIA expression and localization in ECs. The CLIRRTSIC is a novel peptide that could be used for targeted delivery of therapeutics such as siRNAs to pro-atherogenic endothelium.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3002</BiopanningDataSetID>
<Peptides>NHVHRMHATPAY(3)[0.434 ± 0.067, 0.272 ± 0.041]
THAAHMGYPSWW(1)[0.452 ± 0.062, 0.286 ± 0.013]
TKNMLSLPVGPG(1)[0.312 ± 0.023, 0.252 ± 0.030]
WPHNWWPHFKVK(1)[0.312 ± 0.013, 0.329 ± 0.087]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:27168498</Reference>
<Target_Name>Serum from mice with traumatic brain injury (TBI)</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>Each phage clone was evaluated using ELISA against serum samples from uninjured and injured mice. The absorbance was read at 450 nm. Data shown were reproduced from the graph in the published paper. Data in the first column and the second column represent affinity values of phages for serum samples from injured and uninjured mice, respectively.</Affinity_Measurement_Description>
<Brief_Description>To eliminate clones that bind serum from control mice (without traumatic brain injury), the library was preincubated with a 96 well plate (Nunc Immuno Plate, Maxisorp surface) coated with pooled serum from control mice diluted 1:100 in TBS (100 μl).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3003</BiopanningDataSetID>
<Peptides>STYTSVS(2)
SYYTSVS(1)
SHYTSVS(1)
SYYTSVS(1)
VTDTSVS(1)
ATYTSVS(1)
TYTSVS(1)
VTYTSVS(1)
SHLYYVS(1)
NSPWLMT(1)
PNMQSQS(1)
KLRWNQT(1)
YRNTPLS(1)
APPPSPT(1)
PPARHRC(1)
APAQAKS(1)
YLCGSR(1)
LMIRQPD(1)</Peptides>
<Motif>TSVS</Motif>
<Unique_Sequence_Number>18</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:23375098</Reference>
<Target_Name>Helix 69 of Escherichia coli 23S rRNA</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 the positive selection, the phage solution (10 μL of the original library in 100 μL buffer A, 2.0e11 pfu, in which pfu is plaque forming unit) was pipetted into a well having no immobilized target RNA and incubated for 1 h at RT with gentle shaking for prescreening of the library.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3004</BiopanningDataSetID>
<Peptides>TPSHPLT(4)
TSPHPLT(1)
TRSHPLT(1)
TPRHPLT(1)</Peptides>
<Motif>HPL</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:23375098</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>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3005</BiopanningDataSetID>
<Peptides>STYTSVS(11)
NQVANHQ(5)
STYLYCA(1)
PDYTSVS(1)
YYAAESL(1)
IRLPNHQ(1)</Peptides>
<Motif>TSVS</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:23375098</Reference>
<Target_Name>Helix 69 of Escherichia coli 23S rRNA</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 the positive selection, the phage solution (10 μL of the original library in 100 μL buffer A, 2.0e11 pfu, in which pfu is plaque forming unit) was pipetted into a well having no immobilized target RNA and incubated for 1 h at RT with gentle shaking for prescreening of the library.</Brief_Description>
<BiopanningDataSet_Comments>One selected sequence, NQVANHQ, was shown through a bead assay to interact with helix 69. Electrospray ionization mass spectroscopy revealed an apparent dissociation constant for the amidated peptide and helix 69 in the low micromolar range. This value is comparable to that of aminoglycoside antibiotics binding to the A site of 16S rRNA or helix 69. Helix 69 variants (human) and unrelated RNAs (helix 31 or A site of 16S rRNA) showed two to four fold lower affinity for NQVANHQ-NH2. These results suggest that the peptide has desirable features for development as a lead compound for novel antimicrobials.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3006</BiopanningDataSetID>
<Peptides>STYTSVS(8)
NQVANHQ(4)</Peptides>
<Motif>TSVS</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:23375098</Reference>
<Target_Name>Helix 69 of Escherichia coli 23S rRNA</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 the positive selection, the phage solution (10 μL of the original library in 100 μL buffer A, 2.0e11 pfu, in which pfu is plaque forming unit) was pipetted into a well having no immobilized target RNA and incubated for 1 h at RT with gentle shaking for prescreening of the library. For round 4, specific elution was carried out with 30 pmol of H69 RNA in TBST buffer.</Brief_Description>
<BiopanningDataSet_Comments>One selected sequence, NQVANHQ, was shown through a bead assay to interact with helix 69. Electrospray ionization mass spectroscopy revealed an apparent dissociation constant for the amidated peptide and helix 69 in the low micromolar range. This value is comparable to that of aminoglycoside antibiotics binding to the A site of 16S rRNA or helix 69. Helix 69 variants (human) and unrelated RNAs (helix 31 or A site of 16S rRNA) showed two to four fold lower affinity for NQVANHQ-NH2. These results suggest that the peptide has desirable features for development as a lead compound for novel antimicrobials.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3007</BiopanningDataSetID>
<Peptides>CAKATCPAC(26)
CSWQIGGNC(20)
CTVRTSADC(12)
CIGNSNTLC(10)
CIKVGKLQC(2)
CNWGDRILC(2)
CTNANHYFC(2)
CGWSGSLVC(1)
CLYANSPFC(1)
CSISSLTDC(1)
CNWGDRIRC(1)
CNWGDRIEC(1)
CRSANIFTC(1)
CFNMFSRFC(1)
CISAWPTRC(1)
CSISSLTHC(1)
CFLNPTTTC(1)
CKNLTRLAC(1)
CMARYMSAC(1)
CIKVGKVQC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:25366491</Reference>
<Target_Name>Human adenocarcinoma lung cancer cell line A549</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>For in vivo biopanning, a mouse bearing A549-derived xenograft tumor was injected with 1.0e9 pfu of the random library in TBS buffer 200 μl via the tail vein. After 15 min of biocirculation, the mouse was anesthetized by i.p. injection of zoletil (40 mg/kg) plus rompun (10 mg/kg) mixture and perfused with 50 mL of Tris-buffered saline (TBS; 50 mM Tris–HCl (pH 7.6), 150 mM NaCl) to remove non-specific and unbound phages. In subsequent rounds of biopanning to fourth rounds, different concentrations of detergent in the TBS buffer were used to wash out effectively non-specific bound phages. The increasing concentrations of Tween-20 were as follows: 0.1 % for second round, 0.3 % for third round and 0.5 % for fourth round in the TBS buffer. Then tumor tissues were resected from the mouse and homogenized in 1 mL of cold TBS containing 1× protease inhibitor cocktail (Tech and Innovation Co., Ltd, Seoul, Korea) on ice. Bound phages were subsequently eluted from the homogenate by 0.2 M glycine–HCl (pH 2.2) and the mixture was neutralized with 1 M Tris–HCl (pH 9.1).</Brief_Description>
<BiopanningDataSet_Comments>Novel peptides were categorized into four groups according to a sequence-homology phylogenicity, and in vivo tumor-targeting capacity of these peptides was validated by whole body imaging with Cy5.5-labeled phages in various cancer types. The result revealed that novel peptides accumulated only in adenocarcinoma lung cancer cell-derived xenograft tissue. For further confirmation of the specific targeting ability, in vitro cell-binding assay and immunohistochemistry in vivo tumor tissue were performed with a selected peptide (G9, LYANSPF). The peptide was found to bind intensely to lung cancer cells both in vitro and in vivo, which was efficiently compromised with unlabeled phages in an in vitro competition assay. In conclusion, the peptides specifically targeting human lung cancer were discovered in this study, which is warranted to provide substantive feasibilities for drug delivery and imaging in terms of a novel targeted therapeutics and diagnostics.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3008</BiopanningDataSetID>
<Peptides>DPQYTRFHQHPQ[1.443, 0.266]
DQHYTRFHQHFR[1.432, 0.271]
QLGHYDRFHKHP[1.421, 0.277]
SMNPTWLRFHPH[1.247, 0.260]
YPTFERFHTHTP[1.215, 0.250]
SSMLNRFHIHTL[1.231, 0.250]
IPYTRFHDHQYT[1.383, 0.260]
STSASYTRFHSH[1.394, 0.250]</Peptides>
<Motif>Y-x-R-F-H-x-H</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:27191594</Reference>
<Target_Name>Anti-VP3 monoclonal antibody 4A6</Target_Name>
<Template_Name>Capsid protein VP3</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>Each phage clone was evaluated using ELISA against mAb 4A6 and mAb anti-porcine IFN-c (Sigma, StLouis, MO, USA) as a negative control. The absorbance was read at 450 nm. Data shown were reproduced from the graph in the published paper. Data in the first column and the second column represent affinity values of phages for mAb 4A6 and mAb anti-porcine IFN-c, respectively.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Phage clone peptides displayed a consensus sequence of YxRFHxH that mimicked the sequence 82Y/FNRFHCH88, which corresponded to amino acid residues 82 to 88 of VP3 protein of WPVs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3009</BiopanningDataSetID>
<Peptides>SYQYHTLTYTEL[1.404 ± 0.065, 0.147 ± 0.038]
GMAGVQYHPLHL[1.511 ± 0.073, 0.147 ± 0.038]
VNALYSVQYQPL[1.576 ± 0.078, 0.147 ± 0.043]
SYLSVQYEPLLT[1.598 ± 0.086, 0.138 ± 0.043]
ASVDYYTLTDLR[1.451 ± 0.065, 0.142 ± 0.038]
LEKFNMVQGQHT[1.365 ± 0.060, 0.138 ± 0.039]
AYVTYTPLYTTA[1.348 ± 0.065, 0.142 ± 0.038]
SLQYSYYYEEYY[1.343 ± 0.065, 0.138 ± 0.043]</Peptides>
<Motif>SVQYHPL</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:23185456</Reference>
<Target_Name>Anti-gp90 monoclonal antibody A9E8</Target_Name>
<Template_Name>Envelope glycoprotein gp90</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>Each phage clone was evaluated using ELISA against mAb A9E8 and an anti-porcine IFN-c mAb (negative control). The absorbance was read at 490 nm. Data shown were reproduced from the graph in the published paper. Data in the first column and the second column represent affinity values of phages for mAb A9E8 and an anti-porcine IFN-c mAb, respectively.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The mAb A9E8 recognized phages displaying peptides with the consensus motif SVQYHPL. Amino acid sequence of the motif exactly matched 213SVQYHPL219 of the gp90.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3010</BiopanningDataSetID>
<Peptides>SDSLPTPTSNT[1.443 ± 0.098, 0.268 ± 0.060]
SMLTAPPTSRD[1.247 ± 0.093, 0.264 ± 0.064]
HSYPTPRTSSG[1.357 ± 0.102, 0.264 ± 0.064]
VDEYGTALTS[1.417 ± 0.090, 0.264 ± 0.064]
SHTQDPAPTSNV[1.319 ± 0.098, 0.264 ± 0.059]
TQMLPAPDLPS[1.468 ± 0.094, 0.264 ± 0.064]
ATSTQPATSNT[1.506 ± 0.102, 0.264 ± 0.064]
NTLPANVPSN[1.204 ± 0.098, 0.268 ± 0.064]</Peptides>
<Motif>LPAPTS</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:25706372</Reference>
<Target_Name>Anti-VP1 monoclonal antibody 2D10</Target_Name>
<Template_Name>Capsid protein VP1</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>Each phage clone was evaluated using ELISA against mAb 2D10 and an anti-porcine IFN-c mAb (negative control). The absorbance was read at 450 nm. Data shown were reproduced from the graph in the published paper. Data in the first column and the second column represent affinity values of phages for mAb 2D10 and an anti-porcine IFN-c mAb, respectively.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The mAb 2D10 recognized phages displaying peptides with the consensus motif LPAPTS. Sequence alignment showed that the epitope 173LPAPTS178 is highly conserved among the duck hepatitis A genotype 1 virus (DHAV-1) genotypes.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3011</BiopanningDataSetID>
<Peptides>CYWGGTEGAC(9)
CFGAHGVFFC(8)</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:27226142</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor III, IgG Fc receptor III</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>CX8C fUSE5 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The two novel CD16 ligands identified negatively regulate bacterial killing and inflammation.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3012</BiopanningDataSetID>
<Peptides>VVPWAGL(12.5%)
WTVHTLS(25%)
HMFPWRQ(12.5%)
QSWLPSL(8.4%)
GYKDFSA(16.6%)
RILITIP(12.5%)
WASKVAR(8.4%)</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:26896129</Reference>
<Target_Name>Hemagglutinin-esterase, HE</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3013</BiopanningDataSetID>
<Peptides>TPARHIY(16.6%)
TLLRVDN(11.1%)
GSGNAFM(27.7%)
MPLGFKA(16.6%)
NERALTL(16.6%)
VQPIPAT(11.1%)</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:26896129</Reference>
<Target_Name>Fusion protein</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3014</BiopanningDataSetID>
<Peptides>TRRAFGSSFRLS
SAARTLEVHSSS
TSAGDIVVLISL
LSRSYCRPPAPC
EAESRVYRPGTS
SYFPFTYKITRN
FPPIFAEATARS
QTISLPLDSPKR
SGVYKVAYDWQH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:26970402</Reference>
<Target_Name>C-terminal half of aryl hydrocarbon receptor (AhR)</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>Biopanning was performed as follows: HisTag Dynabeads, BSA, and Ph.D.-12 library were incubated in biopanning buffer using a rotating device to preclear the phages. The precleared solution was added to a new tube containing 6His-AHR-N△515 and HisTag Dynabeads. The biopanning process was performed three times to generate the final phage solution. A secondary screening was performed as follows: a LI-COR nitrocellulose membrane (Lincoln, NE) was used for membrane lift to create a mirror image of the individual colonies on the membrane. This membrane was subjected to denaturation/neutralization, and then the membrane was dried and blocked. The blocked membrane was incubated with the IRDye800-conjugated 6HisAHRN△515. After incubation, the membrane was washed, followed by LI-COR Odyssey analysis to detect the colonies bound with AHR-ND515 according to the near IR fluorescence intensity.</Brief_Description>
<BiopanningDataSet_Comments>Eight 12mer peptides, in the form of GFP fusion, suppressed the ligand-dependent transcription of six AHR target genes (cyp1a1, cyp1a2, cyp1b1, ugt1a1, nqo1 and ahrr) in different patterns in Hep3B cells, whereas the AHR antagonist CH223191 suppressed all these target genes similarly. Three of the 12mer peptides (EAESRVYRPGTS, FPPIFAEATARS and TRRAFGSSFRLS) suppressed the 3MC-induced, CYP1A1-dependent EROD activity and the ROS production caused by benzo[a]pyrene. These 12mer peptides suppressed the AHR function synergistically with CH-223191.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3015</BiopanningDataSetID>
<Peptides>SNQLPQQ</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:25761931</Reference>
<Target_Name>Neural stem/progenitor cell</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Screening of the phage library was performed by the BRASIL method, which allows the separation of cell-bound from unbound phage in one step.</Brief_Description>
<BiopanningDataSet_Comments>The peptide with the highest affinity, SNQLPQQ, was expressed in conjunction with a bispecific adaptor molecule. To verify the targeting potential of the specific peptide, green fluorescent protein-expressing Ad vectors were coupled with the adaptor molecule and injected into the subventricular region of adult mice by stereotaxic surgery. An efficient and selective transduction of NSPCs in the SVZ was achieved, whereas hippocampal NSPCs were negative.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3016</BiopanningDataSetID>
<Peptides>RVTGMMLWD(27)
VTGMSLRPD(16)
PVTGMAALA(4)
RLTGMMLWD(3)
RRLVTGMSLY(3)
RVTGMSFII(3)
RLIGMMLWDP(1)
VLTPMMLAW(1)
VVTPMMLAW(1)
VSGMSLRPD(1)
VTGMSLVQG(1)
VSGMSLVHG(1)
VTGMSALAP(1)
RVTGMSISV(1)
GRVTPMSVS(1)
GSVTPMAIV(1)
GAVTPMAIV(1)
MVVTGMALV(1)
VRVTPMILI(1)
VTPMAVRLE(1)
CTGLVRMN(1)</Peptides>
<Motif>RVTGMSLV</Motif>
<Unique_Sequence_Number>21</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>7</Rounds_of_Panning>
<Reference>PMID:27216028</Reference>
<Target_Name>Granzyme-like I</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>X9 T7 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>3017</BiopanningDataSetID>
<Peptides>CSSPIGRHC(8)
CTMSNLKGC(1)
CNNVLSQMC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:27221614</Reference>
<Target_Name>Human non-muscle-invasive bladder cancer cell line BIU-87</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>Tumor-bearing mice were intravenously injected with phage peptide library via the tail vein.</Brief_Description>
<BiopanningDataSet_Comments>The isolated phage display peptide (CSSPIGRHC, named NYZL1) was tested in vitro for its binding specificity and affinity. Accumulation into xenograft tumors in a nude mouse model was analyzed with FITC-labeled NYZL1. NYZL1, with strong tumor-homing ability, was identified by in vivo phage library selection in the bladder cancer model. The NYZL1 phage and synthetic FITC-labeled NYZL1 peptides bound to tumor tissues and cells, but were hardly detected in normal control organs. Notably, accumulation of FITC-NYZL1 in bladder tumor cells was time-dependent. Biodistribution studies of xenografts of BIU-87 cells showed accumulation of injected FITC-NYZL1 in the tumors, and the bound peptide could not be removed by perfusion after 24 h. The mouse model of bladder tumor showed increased fluorescence intensity in the tumor-bearing bladder in comparison with normal bladder tissues after 4-6 h. NYZL1 may represent a lead peptide structure applicable in the development of optical molecular imaging.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3018</BiopanningDataSetID>
<Peptides>FPWTEPSYKQGD
FPWTEPLYKYGE
FPWTEPSYKYGD
MPWKESAWLEKI
MPWTEPNYLLTQ
IPWKESACLAKI
APWLEGSYKTVY
KQFSALPFNFYT
SEFPRSWDMETN</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:27209258</Reference>
<Target_Name>Human prostate cancer cell line PC3				</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>3019</BiopanningDataSetID>
<Peptides>CNLSSSWIC(5)
CPSSQRFFC(2)
CLNSLSRHC(1)
CSLNSDLFC(1)
CTSATSNSC(1)
CVQSNPLSC(1)
CSNNLLHNC(1)
CRPLSFGHC(1)
CSSNLPLSC(1)
CSSHSWRLC(1)
CLPALTRSC(1)
CTQLARSAC(1)
CLAPQSHRC(1)
CSPNAPNSC(1)
CHGPVSRSC(1)
CSMLSVAAC(1)
CSQWSPHRC(1)
CQATLHLGC(1)
CPSVPHAHC(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:27313992</Reference>
<Target_Name>Anti-GRA2 monoclonal antibody C3C5</Target_Name>
<Template_Name>Dense granule protein 2, Protein GRA 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>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></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3020</BiopanningDataSetID>
<Peptides>YTHNEKPSSDTH(5)[0.945 ± 0.051]
YTVPDNHKYSAH(3)[0.900 ± 0.064]
THPWQVSTINFK(3)[0.956 ± 0.055]
IHKDKNAPSLVP(2)[0.957 ± 0.048]
DVFPPRSHADEL(1)[0.957 ± 0.056]</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>DOI:10.1007/s10989-013-9367-7</Reference>
<Target_Name>Gastric cancer cell line SGC-7901</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>Each phage clone was evaluated using ELISA against SGC-7901 cells. Phage clone displaying irrelevant peptide (PIRPs) and PBS were used as negative controls. Plates were read by using a microplate reader (BioRad Model 550, Hercules, CA) at 450 nm. Data shown were reproduced from the graph in the published paper. The affinity value of phages displaying PIRPs for SGC-7901 cells was 0.032. And the affinity value of PBS for SGC-7901 cells was 0.021.</Affinity_Measurement_Description>
<Brief_Description>The 12-mer phage peptide library was preincubated with HEK293 cells to remove any HEK293 cells-binding phage before being added to the SGC-7901 cells-coated cultures.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3021</BiopanningDataSetID>
<Peptides>YFPYSHTSPRQP[1.304, 0.183]
AYKYTSALPAEA[0.970, 0.200]
SLTLMNSPLGAS[1.161, 0.161]
MLTLSLNPTNSA[0.517, 0.200]</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:27246497</Reference>
<Target_Name>Protein EaeB</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 binding affinity of the positive phage clones and control vcsM13 to EspB and 6× His was determined by ELISA. Absorbance was measured at 450 nm. Phage clones were considered to possess high affinity for EspB if their OD values were two-fold greater than those of the control phage and peptide. Data shown were reproduced from the graph in the published paper. The binding affinity of the control vcsM13 to EspB and 6× His was 0.230 and 0.183, respectively. Data in the first column and the second column represent affinity of phages to EspB and 6× His, respectively.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3022</BiopanningDataSetID>
<Peptides>NPMIRRQ(5)[1.349 ± 0.130]
MRMTIIN(3)[1.458 ± 0.160]
LRLRNTR(1)[1.686 ± 0.172]
SHLRHRI(1)[1.797 ± 0.142]
KLPLTTK(1)[1.241 ± 0.187]
PIKTNRK(1)[1.134 ± 0.041]
KPTIPTK(1)[1.499 ± 0.081]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:27313733</Reference>
<Target_Name>Human ovarian cancer cell line HO-8910</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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The binding affinity of the positive phage clones to HO-8910 cells was determined by ELISA. The M13K07 phage and phosphate-buffered (PBS) saline were used as negative controls. Absorbance was measured at 490 nm. Data shown were reproduced from the graph in the published paper. The binding affinity of M13K07 phage and PBS to HO-8910 cells was 0.041 ± 0.015 and 0.061 ± 0.031, respectively.</Affinity_Measurement_Description>
<Brief_Description>The phage peptide library was preincubated with Chinese hamster ovary cell line (CHO) to remove any CHO cells-binding phage before being added to the HO-8910 cells-coated tubes.</Brief_Description>
<BiopanningDataSet_Comments>Immunofluorescence and immunohistochemical assays revealed that the phage clone with the sequence of NPMIRRQ was able to bind to ovarian cancer cells and tissues, and not those of cervical cancer. The peptide may be a potential agent for the diagnosis of ovarian cancer.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3023</BiopanningDataSetID>
<Peptides>SGVYKVAYDWQH(5/34)
SSLELSRSSAAS(2/34)
QTFSRPDWTMYL(2/34)
DPDDTHIMRLLY(1/34)
XKSTASMFTTAR(1/34)
GSAARWPFSVTL(1/34)
LTNTSQLQTRIG(1/34)
SQDIRTWNGTRS(1/34)
IEINATRAGTNL(1/34)
SMRASYPMPTFI(1/34)
GLHTSATNLYLH(1/34)
FPGLFEMVESLN(1/34)
VNMVPLGKNVVQ(1/34)
IDAHFGLRLVND(1/34)
GSGASYQVWRPM(1/34)
MHYGTYTVGYKQ(1/34)
VLKEASHLPYSG(1/34)
GDYGDGFRLLYI(1/34)
VAGLKEQAELDY(1/34)
TSWNMGLTYAGQ(1/34)
VLTNIARGEYMR(1/34)
GQAGGEWILHPL(1/34)
AASSGVTVTLPT(1/34)
GESVSRIDVGSA(1/34)
TTVTGASFSAAY(1/34)
IEASFYDAPRGG(1/34)
KASGSPSGFWPS(1/34)
GSWGLNDSHSYR(1/34)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>28</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:27486695</Reference>
<Target_Name>Human blood-brain barrier (BBB) cellular model</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>From the panning experiment of a 12-mer library, the SGVYKVAYDWQH (SGV) peptide sequence was selected and internalisation studies suggested that SGV internalises through a clathrin-mediated mechanism and that it increases the uptake of a cargo in endothelial cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3024</BiopanningDataSetID>
<Peptides>SGVYKVAYDWQH(2/31)
KLNSLDSGMRLV(1/31)
AFNPSTPHLRLI(1/31)
GLTGDLSLNTAT(1/31)
ETLSSYVKKPGH(1/31)
AIYMDTGPLAGR(1/31)
SLPVGSSSDGWV(1/31)
LPLSYNDKARAE(1/31)
RVSIESHHLDHY(1/31)
DGAVSYLQLRVT(1/31)
GLHTSATNLYLH(1/31)
FIPFDPMSMRWE(1/31)
LDQLPCCWSKTG(1/31)
WVNDTNSPLVPR(1/31)
MLAPRQTEHGRI(1/31)
LMKSPQPLHSSR(1/31)
MHPNAGHGSLMR(1/31)
GQAPSVPFFASI(1/31)
NERNHEIMMAQA(1/31)
HEMYSSFGALTV(1/31)
NMANYSAISSRW(1/31)
STPIFAEATARS(1/31)
HSADINVGSRTR(1/31)
DEAAYGLKLPGK(1/31)
DLGRASSILPSG(1/31)
GLFGNEARTAST(1/31)
YTNDHSRPKLVP(1/31)
SVNSDHTSMRSH(1/31)
AVMPRDHVLNAT(1/31)
LHRQDNYLAASX(1/31)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>30</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:27486695</Reference>
<Target_Name>Human blood-brain barrier (BBB) cellular model</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>From the panning experiment of a 12-mer library, the SGVYKVAYDWQH (SGV) peptide sequence was selected and internalisation studies suggested that SGV internalises through a clathrin-mediated mechanism and that it increases the uptake of a cargo in endothelial cells.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3025</BiopanningDataSetID>
<Peptides>LAKPHTENHY(4/32)[1.02 ± 0.11]
QNPIQKIIY(1/32)[0.81]
LAKPHTENHLLT(1/32)[1.16]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:27491899</Reference>
<Target_Name>The envelope protein Ampho4070A</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 binding activities of the positive phage clones to the envelope protein Ampho4070A expressed by retrovirus like particles were measured by phage ELISA. The OD450 values were measured and data shown were reproduced from the Fig. 1b in the reference.</Affinity_Measurement_Description>
<Brief_Description>In order to eliminate unspecific binders several depletion steps were incorporated in the panning campaigns using the VLP null particles as well as non-coated plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>