<result><BiopanningDataSet><Item><BiopanningDataSetID>526</BiopanningDataSetID>
<Peptides>KHLPLYR(10)
KHNWPPP(8)
FHEPKYR(7)
GHIAKYR(6)
GHLWKYV(2)</Peptides>
<Motif>HLP</Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18725193</Reference>
<Target_Name>Omalizumab</Target_Name>
<Template_Name>Ig epsilon chain C region</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 second and third round of selection, the library was precleared on trastuzumab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>527</BiopanningDataSetID>
<Peptides>PLLQATL(2)
RKPGKPV(1)
TLHSAQA(1)
HNRPRNN(1)
RHTHRSH(1)
TAPGVST(1)
NLTLAWR(1)
HTTHMYL(1)
WSAPVPN(1)
SFRPTPP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:20414975</Reference>
<Target_Name>Heparin-binding growth factor 2, HBGF-2</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>PLLQATL showed high homology to the immunoglobulin-like (Ig-like) domain III (D3) of high-affinity bFGF receptors, FGFR1 (IIIc) and FGFR2 (IIIc). Synthetic PLLQATL peptides mediate strong inhibition of bFGF-induced cell proliferation and neovascularization.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>528</BiopanningDataSetID>
<Peptides>CAWYEWPC(12)
CAWYQFPC(6)
CVWWQWPC(1)
CPWFQWPC(1)
CKWFQWPC(7)
CFWVNTDC(1)
CLYLSIRC(1)</Peptides>
<Motif>x-W-[FYW]-[QE]-[WF]-P</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:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Cys6 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments>Among 29 selected clones, seven different amino acid sequences were found.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>529</BiopanningDataSetID>
<Peptides>CCSVRGSAWAC(2)
CILTIHGPLQC(2)
CGARLAMAVAC(1)
CRDCVVACLGC(1)
CSMGLGGTSLC(1)
CGAPNLSRLLGC(1)
CGLGYRTAHIC(1)
CTLRLGVGVRC(1)
CHPHFPWATSC(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:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Cys9 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>530</BiopanningDataSetID>
<Peptides>WAWVWLTETAV(23)
AVTFKFTGTDL(2)
GSSHASLRYPA(1)
LLSFAGRSPSC(1)
LSGRSSGWRFS(1)
RLRFVVHESSG(1)
CPLGLLIHTSC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>NNK11 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>531</BiopanningDataSetID>
<Peptides>VGGCPWFQWPCKGQ(2)
DQECPWFQWPCGAA(2)
TRVCPWFQWPCVTG(2)
VMKCPWFQWPCDAL(1)
RVRCPWFQWPCGMH(1)
SRSCPWFQWPCGSV(1)
TPNCPWFQWPCLKS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Evo1 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>532</BiopanningDataSetID>
<Peptides>TDRMCRWFQWPC(1)
NSRDCAWFQWPC(1)
GEDRCLWFQWPC(1)
NKDECRWFQWPC(1)
IDSRCHWFQWPC(1)
GGMKCWWFQWPC(1)
GCNACAWFQWPC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Evo2 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>533</BiopanningDataSetID>
<Peptides>CPWFQWSDSGCS(4)
CPWFQWPCLSHA(2)
CPWFQWPCGARV(2)
CPWFQWMLGCV(1)</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:18957413</Reference>
<Target_Name>Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a</Target_Name>
<Template_Name>Fc domain of IgG (IGHG1,IGHG2,IGHG3,IGHG4)</Template_Name>
<Structure_of_Target_Template_Complex>3RY6,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Evo3 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the first round, FcγRIIA-R134-GST immoblized by precoated with goat anti-GST polyclonal antibody was used for panning. For other rounds, MaxiSorp strips coated FcγRIIA-R134-GST was used.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>534</BiopanningDataSetID>
<Peptides>TDTCLMLPLLLGCDEE
DPICWYFPRLLGCTTL
WYPCYIYPRLLGCDGD
GNICMLIPGLLGCSYE
VNSCLLLPNLLGCGDD
TPVCILLPSLLGCDTQ
TVLCSLWPELLGCPPE
TFSCLMWPWLLGCESL
FGTCYTWPWLLGCEGF
SLFCRLLLTPVGCVSQ
HLLVLPRGLLGCTTLA
TSLCSMFPDLLGCFNL
SHPCGRLPMLLGCAES
TSTCSMVPGPLGAVSTW
KDPCTRWAMLLGCDGE
IMTCSVYPFLLGCVDK
IHSCAHVMRLLGCWSR</Peptides>
<Motif>T-x(2)-C-x(2)-P-x-L(2)-G-C-x(2)-E</Motif>
<Unique_Sequence_Number>17</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18957574</Reference>
<Target_Name>High affinity immunoglobulin gamma Fc receptor I, IgG Fc receptor I</Target_Name>
<Template_Name>Ig gamma-1 chain C region</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>CPEP-8 phage display library (X3CX8CX3)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These peptides were able to inhibit IgG1 binding to FcγRI. In soluble form, these peptides antagonize superoxide generation mediated by IgG1. In complexed form, they trigger phagocytosis and a superoxide burst. Unlike IgG, these peptides are strictly FcγRI-specific among the FcγRs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>535</BiopanningDataSetID>
<Peptides>HSEAETGPP[2.16 ± 0.18]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19480736</Reference>
<Target_Name>Serum of a pars planitis patient</Target_Name>
<Template_Name>Proline-rich transmembrane protein 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>J404 phage display library (X9)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance was measured at 492 nm. Data were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>One hundred clones were randomly selected from a phage display library after three panning rounds using serum proteins from a PP patient. The immunologic response level of 100 clones selected were determined with a major number of patients, only the clone 83 was recognized stronger in PP patients sera than in healthy sera (PP vs. healthy; P&lt;0.05). An identical amino acid sequence to HSEAETGPP is found in the human proline-rich transmembrane protein 2 which has not been related with eye diseases.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>536</BiopanningDataSetID>
<Peptides>SSVLYGGPPSAA[0.65]
LPQNVWLHGWHT[0.46]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:19299727</Reference>
<Target_Name>Anti-hstone H1 monoclonal antibody 16G9</Target_Name>
<Template_Name>Histones H1 from calf thymus</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>Specific binding of 16G9 mAb to KLH-conjugated SSVLYGGPPSAA and LPQNVWLHGWHT were determined by ELISA. KLH was used as an internal control. Increasing amounts (0–0.5 μg/ml) of 16G9 mAb were added to the wells. Bound 16G9 mAb was detected using biotin-conjugated anti-mouse IgM Ab. Peroxidase-conjugated streptavidin was added and the streptavidin-biotinylated peroxidase complex was detected by ABTS substrate solution. Multiskan Ascent was used to determine absorbance at 405 nm. The A405 values of the binding of 16G9 in the concentration of 0.5 μg/ml to the peptides were shown and the data were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The binding of 16G9 mAb to histone H1 was inhibited by SSVLYGGPPSAA, which was also recognized by rat tolerogenic post-orthotopic liver transplantation serum. The binding of 16G9 mAb to SSVLYGGPPSAA was inhibited by histone H1. Abs induced by SSVLYGGPPSAA immunization inhibited Con A-stimulated splenocyte proliferation, and the inhibition was neutralized by preincubation with SSVLYGGPPSAA. Splenocytes stimulated by anti-CD3 Ab were inhibited by SSVLYGGPPSAA-induced Abs. SSVLYGGPPSAA immunization in rats before heterotopic heart transplantation resulted in significant prolonged allograft survival.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>537</BiopanningDataSetID>
<Peptides>CPSGHTKAC(2)
CTPGKPHSC(2)
CGTHSSRIC(1)
CLGTQNKEC(1)
CKAASANIC(1)
CLPTRHMAC(1)
CLSAVHNMC(1)</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:18985310</Reference>
<Target_Name>CD40 ligand, CD40-L</Target_Name>
<Template_Name>Tumor necrosis factor receptor superfamily member 5</Template_Name>
<Structure_of_Target_Template_Complex>3QD6,</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>The immobilized recombinant hCD154-muCD8 was used as the target. To eliminate potential non-specific binding of phage clones with affinity for plastic or muCD8, two negative selections were performed with plastic and a non-related recombinant fusion protein hCD153-muCD8.</Brief_Description>
<BiopanningDataSet_Comments>Nine phage clones were selected for the ability to bind CD154 expressed on the surface of J558L cells transfected with human CD154. From the nine selected phage clones, seven different amino acidic sequences were obtained and synthesized. All the peptides specifically bound CD154 expressed on J558L. However, only the peptide CLPTRHMAC was found to recognize the active binding site of CD154, as it competed with the blocking anti-CD154 antibody.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>538</BiopanningDataSetID>
<Peptides>VQATQSNQHTPR(2)
VQATPRLQHTPR(1)
VQATTVQIQHAP(1)
VQAIQSNQLTPR(1)
VQAGQSNAHTAG(1)
VQARQSNQHTPR(1)
VQNYQSNQHTPR(1)
AQALGLSAISPR(1)
AQGPPSKQHSPP(1)
EQATPRNHNSPP(1)
TFATQSNQHTPR(1)</Peptides>
<Motif>VQATQSNQHTPR</Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:19284521</Reference>
<Target_Name>Agglutinin</Target_Name>
<Template_Name>N-acetylgalactosamine</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>Phage particles that were eluted from the lectin with free GalNAc were considered to have been bound to a GalNAc-binding site.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>539</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(0.75)
NHNTSTWAAYST(0.125)
TLPSPHSLLTVH(0.125)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaAs(100)</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>540</BiopanningDataSetID>
<Peptides>SSMEPDPFLALY(0.666)
SSVEPGPFLALY(0.111)
SSMYPELFLALY(0.111)
SSMNPELFLALY(0.111)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface InAs(100)</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>541</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(0.5)
MSGDIISLAPTG(0.125)
GPFFPKSLTTTS(0.125)
NAPLSHIPENPR(0.125)
SISAMPAPANSS(0.125)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaN(0001)</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 affinity of the SVSVGMKPSPRP peptide towards the GaN(0001) surface is drastically diminished in the presence of water, whereas when PBST has been used as solvent, the adhesion of this peptide was demonstrated. Influence of the eluent proticity and dielectric constant were confirmed by the use of various solvents. The MALDI signal of the peptide adsorbed onto the GaN(0001) decreases in intensity when the dielectric constants of the employed solvents increase. The media with a high dielectric constant reduces the force acting between the peptide and the GaN(0001) and the molecules are washed out of the surface. When rinsing with 1M NaCl directly or after a previous water washing, there was no peptide left on the surface, indicating towards the electrostatic nature of the interactions between the peptide and the GaN(0001) surface.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>542</BiopanningDataSetID>
<Peptides>LLADTTHHRPWT(0.444)
SVSVGMKPSPRP(0.111)
HHLSXKTVGAST(0.111)
HDSLLHPARSAP(0.111)
FAPEDLPNYPQR(0.111)
HSKPQQPPFVXS(0.111)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface ZnSe(100)</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>543</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(0.285)
LVKDIRGAIPYM(0.142)
NNQLSFPAGTTR(0.142)
HPQNTFAANLRP(0.142)
TSANGKPPALML(0.142)
SNIAPGVLPRST(0.142)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface ZnTe(100)</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>544</BiopanningDataSetID>
<Peptides>APWHFTRVPALV(0.2)
INPMVMSNPNNR(0.2)
STFSTNWPSTPT(0.2)
TTTNWQLSAPAP(0.2)
APQHMIWPKPTA(0.2)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaAs(111)A
</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>545</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(0.666)
AQDLNYVRLGPS(0.333)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaAs(111)A
</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>546</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(1.0)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaAs(111)A
</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>547</BiopanningDataSetID>
<Peptides>DHPTNQLAVPSS(0.125)
QHMDKLTHRKPH(0.125)
HNIHAITPLTPI(0.125)
ASASHLNKRFMT(0.125)
STTTSNLLNYRI(0.125)
SPLTSPGPHVSS(0.125)
HSNPHEAIRASR(0.125)
HKHTTTPLFTSR(0.125)</Peptides>
<Motif></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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaSb(100)
</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>548</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(1.0)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaSb(100)
</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>549</BiopanningDataSetID>
<Peptides>HNQTAPHLPRQS(0.2)
SVSVGMKPSPRP(0.8)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:19634182</Reference>
<Target_Name>Semiconductor crystalline surface GaSb(100)
</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>550</BiopanningDataSetID>
<Peptides>AYPQFPNLRTSL(0.142)
GTLNSSVEPPLG(0.142)
NSNSYRVPHGTM(0.142)
IPIGPHIGLVGP(0.142)
APESMMIIDPGF(0.142)
ISTPLSKSPTRL(0.142)
YSPPKTTLPAHS(0.142)</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:19634182</Reference>
<Target_Name>Semiconductor crystalline surface CdSe(100)
</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></BiopanningDataSet></result>