<result><BiopanningDataSet><Item><BiopanningDataSetID>3301</BiopanningDataSetID>
<Peptides>YSLHNAGPWSLQ[0.29]</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:29433534</Reference>
<Target_Name>Immunoglobulin G(IgG) of patients with Rheumatoid arthritis-Secondary Sjögren’s syndrome(RA-sSS)</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>Antibody reactivity against peptides was measured using a solid-phase ELISA and the color intensity was measured at 450 nm.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Phage clones with the sequence YSLHNAGPWSLQ specifically bound to the IgGs of patients with Rheumatoid arthritis-Secondary Sjögren’s syndrome(RA-sSS), which was confirmed by three rounds of screening with the same pooled IgGs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3302</BiopanningDataSetID>
<Peptides>ARGRRG
GRSGRG
ARGRGR
RSGRAG
ARGGGR
RSGGRG
RGRSGG
GRGARG
AVGRGR
ARGGRG
VGRSRG
RVRGRG
RGRGGR
VGRARG
GRAAGR
SVGRAR
ARGRLG
GRSGGR
RGARAG
PRGRRG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6722</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:29434246</Reference>
<Target_Name>Thrombin from prothrombin[328-622]</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>X6 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Out of 5.3 × 106 unique peptide sequences identified following thrombin selection, 6722 peptides were significantly enriched, and identified.</Brief_Description>
<BiopanningDataSet_Comments>Analysis of selected phage sequences confirms a general preference for Arg and exclusion of acidic amino acids in the cleaved peptides. Arg was the dominant amino acid within the most significantly cleaved peptides, consistent with the known requirement at P1 of thrombin substrates.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3303</BiopanningDataSetID>
<Peptides>AVLGGG
LGSVAE
REWGAL
SVRWVG
HGLSAV
ALTVAG
AWMRLG
GLAAVR
GWGAVR
SVAAWR
MGRWGV
TSSVSL
ASVMVV
LSTAVG
VVAGGV
TLVRVA
VVGGWG
AVRLSV
GWGVAG
RLVWGA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>95</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:29434246</Reference>
<Target_Name>A disintegrin and metalloproteinase with thrombospondin motifs 13(ADAM-TS 13)</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>X6 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Compared with thrombin, ADAMTS13 appears to exhibit narrow substrate specificity, since VWF is its only known substrate11. Consistent with this observation, only 96 cleaved peptides were identified from the random peptide library following overnight selection by ADAMTS13.</Brief_Description>
<BiopanningDataSet_Comments>Although cleaved peptides preferentially contained bulky hydrophobic amino acids, no obvious motif was observed, consistent with previous studies that demonstrate poor recognition of short peptidyl substrates by ADAMTS13.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3304</BiopanningDataSetID>
<Peptides>LELYLS
IQLFLA
LRYSSM
LVYMHG
LVPFLS
LLGYTA
RLRYFL
IMMFLG
LVTYVS
PRYYLS
LAYSRN
LIMLLL
LRHYFM
FTLFMV
LTYMRL
VTYMVT
LHYLNY
LTFLLF
LRYRDS
LRFVTR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1670</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:29434246</Reference>
<Target_Name>A disintegrin and metalloproteinase with thrombospondin motifs 13(ADAM-TS 13)</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>VWF73(P3-P3′) phage display library(X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Following treatment of the VWF73(P3-P3′) library with ADAMTS13, 1670 cleaved peptides were detected.</Brief_Description>
<BiopanningDataSet_Comments>Bulky aliphatic amino acids were preferred in the enriched peptide pool, whereas acidic amino acids, as well as proline and cysteine, appeared to antagonize ADAMST13 substrate recognition. The native amino acid sequence for VWF within this interval (Leu-Val-Tyr-Met-Val-Thr) was among the top peptides identified (pFDR = 8 × 10−5), and none of the most significantly cleaved peptides exhibited faster substrate performance than wild type VWF73. As a result, peptides with lower P-values than wild type VWF73 are not necessarily cleaved more efficiently.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3305</BiopanningDataSetID>
<Peptides>GDALFSVPLEVY
SIDDQRDVAEFA
TLHQPPSSANWI
PIDDQRDLAEFA
FTPGGNTYAGQP
SIDDQRDVGEWG
SMCCMTSVSDQP
AVSPPSTIWVPN
VTADSQSPSNQV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:29435721</Reference>
<Target_Name>Cervical cancer</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>Specific phages targeting cervical cancer in vivo were selected with the cervical cancer xenograft model by screening the Ph.D.™-12phage display library for three rounds.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3306</BiopanningDataSetID>
<Peptides>KQNLAEG
STLGPLF
IQQRGEA</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:29435721</Reference>
<Target_Name>Cervical cancer</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>Specific phages targeting cervical cancer in vivo were selected with the cervical cancer xenograft model by screening the Ph.D.™-C7C phage display library for three rounds.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3307</BiopanningDataSetID>
<Peptides>VHWDFRQWWQPS(19)
LNFPMPSRPHSS(5)
QSLPWCYPHCVT(3)
WSPISGKFFQRF(2)
NQLLTQRTPFQD(1)
SSNVISPFEQLL(1)
WVPWSTPFWLQQ(1)
NSPSGLIGWTSR(1)
WVPWSYEYFVST(1)
GPYVLGEHLRSN(1)
SPLWSGWALEIL(1)
SFTWLHGSLTER(1)
SNTQNVYWERWI(1)
RFPGPIEPDLRF(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>14</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:29447281</Reference>
<Target_Name>Insulin-degrading enzyme</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>3308</BiopanningDataSetID>
<Peptides>SWMSIHL(3)
SWWNIHL(2)
NAGHLSQ(2)
NWMNIHM(1)
SKNFPRN(1)
DWMRIWN(1)
IHSPTAL(1)
LPWPLSL(1)
SWWMIHH(1)
LWWQLWL(1)
GFTTTFV(1)
SWWSIHV(1)
LLLLNNT(1)
NWWTIHN(1)
NSIKKWS(1)
ISSSINH(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:29447281</Reference>
<Target_Name>Insulin-degrading enzyme</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3309</BiopanningDataSetID>
<Peptides>GVIHRNDQWTAPGGG
DRWVARDPASIFGGG
SVMNTSTKDAIEGGG</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:29463859</Reference>
<Target_Name>MoS2</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>3310</BiopanningDataSetID>
<Peptides>LGDLHNRDNNSA(1)
HSRTDYVQASYP(1)
GLHTSATNLYLLH(5)
GDGNSVLKPGNW(1)
TASDVPRSRPHS(1)
SGVYKVAYDWQH(5)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:29473787</Reference>
<Target_Name>Mouse heart</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>A total of three pannings were performed. Briefly, at day 21 after induction of EAM, animals received an intravenous injection through the tail vein with either a linear 12 amino acid (AA) peptide phage library or an empty phage at a concentration of 1e9 plaque-forming units (pfu)/μl of PBS.For each panning, animals were divided into the following treatment groups: MyH PhD, MyH Cont,PBS PhD and PBS Cont. The hearts for each of the four treatment groups were weighed, pooled together and homogenized. The resulting homogenate solution for each treatment group was then used to amplify, purify and titer the phages that bound to the hearts in each treatment condition. The phages isolated in panning 1 were injected at 1 × 109 pfu/μl of PBS (110 μl total volume) to animals in the same treatment group in panning 2, and the phages isolated in panning 2 were injected at same concentration and volume to animals in the same treatment group in panning 3.</Brief_Description>
<BiopanningDataSet_Comments>We identified one peptide, MyH-PhD-05, that targets severe myocarditis in vivo.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3311</BiopanningDataSetID>
<Peptides>VHWDFRQWWQPS(15)[1.00±0.05]
AWYSNLLPLARF(1)[1.00±0.05]
LPAQVGQGPLGT(1)[NT]
WFPTSRWTSGWI(1)[NT]
VDARYWTRGTYM(1)[NT]
AKHPDHPLTVGG(1)[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:29046922</Reference>
<Target_Name>Transferrin receptor protein 1</Target_Name>
<Template_Name>Iron-loaded human transferrin</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 geo mean fluorescence values of gradient concentration samples were fitted to the equation (Y = BmaxX/(Kd + X)), and the Kd was used to evaluate the affinity of these peptides.Compared with these peptides, Y1 and Y2 have the comparable affinity at the micromole range, except peptide THRPPMWSPVWP, the Kd of which is low, indicating that the binding of peptides Y1 and Y2 to CD71 is 20 times higher than their binding to other proteins and 8.7 times higher than their binding to protein-free beads.</Affinity_Measurement_Description>
<Brief_Description>After four rounds of selection, the bound phages were collected and used for a counter selection.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3312</BiopanningDataSetID>
<Peptides>HSVGNFWSDYSKYLDSRRAQDFVQWLMLT
HSQGTFTSDYSKYVEDRRAHDFVQWLMNT
HSQGTFTSDYRKYLDERAAWDFVQWLMNT
HSQGTFTSDYSKYLDIGRAQDFVQWLLNT
HSQGTFTSDYSKYLDSLMAQDFVQWLMST
HSQGTFTSDYSKYLDWRRAQDFVQWLLNT
HSQGTFTSDYIKLLDSRRAQDFVQWLMNT
HSQGTFTSDYSKYLDARRAQDFVQWLIRT
HSQGTFTSDYSKYLDVRRAQDFVQWLMNT
HSQGTFTSDYSKYLDELRAYDFVQWLMNT
HSQGTFTSDYSKYLDSRRAHDFVQWLLNT
HSQGTFTSDYSKYLDSRRAQDFVQWLMNP
HSQGTFTSDYSKYLDSRRAQDFVQWLINY
INHEQWAFTSDYSKYLDSRRAQDFVQWLMNT
ASMFTFFSDYSKYLDSRRAQDFVQWLMLT
HSQGTFLSDYSKLLDSRRAQDFVQWLMQT
HSQGTFLHDYYYYLDSRRAQDFVQWLMDT
HSQGTFTSDYSKYLDSIRAQDFVQWLMDT
HSQGTFTSDYSKYLDSRRAQDFVDWLMNE
HSQGTFTSDYSKYLDSRRAQDFVQWLINT
KALGQFTFTSDYSKYLDSRRAQDFVQWLMNT
HSQGTFFSDYSHWLDSRRAQDFVQWLMNT
HSQGTFTSDYSKYLDWRRAQDFVQWLQNT
HSQGTFTSDYSKYLDSKRAHDFVQWLLNT
HSQGTFTSDYSKYLDSRRAQDFWIDLMNT
HSQGTFTSDYSKYLDSRRAQDFVMTSMNT
HSQGTFTSDYSKYLDSRRAQDFVEWLMNN
HSQGTFTSDYSKYLDSRRAQDFVDWLINS
HSHGTFTSDYSKYLDSRRAQDFVQWLMTT
HSQGIFFSDYSKYLDSRRAQDFVQWLMNT
HSQGTFTSDYSWYLDSRRAQDFVQWLMNT
HSQGTFTSDYSKYLDMQRAHDFVQWLMNT
HSQGTFTSDYSKYLDSRMAYDFVQWLMNT
HSQGTFFSDYSKYLDSRRAQDFVQWLLET
HSQGTFTSDYSKYLDSRRAQDFVQWLLDS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>35</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:29330364</Reference>
<Target_Name>glucagon receptor(GCGR-) and glucagon-like peptide-1 receptor(GLP1R-)overexpressing 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>X7FTSDYSKYLDSRRAQDFVQWLX2T, X7SDYSKYLDSRRAQDFVQWLX2T, HSQGTFX7LDSRRAQDFVQWLX2T, HSQGTFTSDYSKYX7DFVQWLX2T and HSQGTFTSDYSKYLDSRRAQX9 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>1e11 phages of the Library Mix were used for the first round of selection on GCGR+ and GLP1R+ overexpressing HEK293 cells, after depletion on naïve cells. Four rounds of selection were carried out, with two different selection schemes: in Scheme 1, the first round was made on GCGR+ cells, followed by a second round on GLP1R+ cells, a third round on GCGR+ cells, and a fourth round on GLP1R+ cells; in Scheme 2, the order of the cells was inverted. Briefly, phage particles were blocked, then incubated with 1e7 naïve cells previously resupended in MPBS for 1 additional hour in a rotary mixer. Cells were  incubated with either GLP1R+ or GCGR+ cells, resupended into 0.5 mL of MPBS for 1hr in a rotary mixer. After incubation. The day after the culture was centrifuged at 4200 rpm for 45 min at 4 °C, the supernatant was recovered and used to perform the next round of selection. The Library Mix was selected alternatively on GCGR+ and GLP1R+ HEK293 overexpressing cells in each round. For selection on GCGR+ and GLP1R+ cells, the five libraries were pulled (‘Library Mix’) and selected together.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3313</BiopanningDataSetID>
<Peptides>DSSAVCWAFPHHPLCHMKAT[0.15][4.98]
ADADMCWFFPTSPWCH[0.92][0.67 ± 0.62] 
DLSAVCWAFPWDPECH[0.03][0.016 ± 0.013]
DSSAVCWAFPYLPECH[0.17][0.048 ± 0.018]
DISAVCWAFPFDPECH[0.25][0.039 ± 0.018]</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:29329326</Reference>
<Target_Name>Avi-tagged interleukin-17A</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>IX104 phage display library(X5CX8CX5)</Library_Name>
<Affinity_Measurement_Method>ELISA,Surface plasmon resonance (SPR)</Affinity_Measurement_Method>
<Affinity_Measurement_Description>BIAcore T200 was used to determine binding affinity and kinetics of the peptides to IL-17A. Avitagged IL-17A was captured to streptavidin sensor chip.For each SPR run, the sensor was first conditioned by 8 cycles of blank prior to sample injections.The resulting sensorgrams of the concentration series of a same peptide were fitted globally to extract binding kinetics and affinity with BIAcore T200 Evaluation Software 2.0 using a 1:1 binding model. Pure peptides from the two libraries were assayed in AlphaLISA format to investigate the potential for disruption of the IL-17A/IL-17RA cytokine-receptor interaction in a biochemical format. In general, the IC50 values determined by AlphaLISA agreed quite closely with the KD values determined through SPR analysis.As was observed in SPR for this family, the differences in AlphaLISA activity between the affinity matured peptides were not significant, with several peptides having IC50's in the 0.2 to 2.0 μMrange.</Affinity_Measurement_Description>
<Brief_Description>IX104 phage display library(X5CX8CX5) consisting of 18 random amino acids were selected against 100 nM of Avi-tagged IL-17A. After three rounds of selection were completed, the eluted phage pool was deconvoluted by filter-lift.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3314</BiopanningDataSetID>
<Peptides>AYECPRLEYDMFGALHCLPS[12.30][61.7]
CPRLEYDMFGALHCL[4.06][5.3 ± 2.5]
CLDLQYDPWGALHCI[2.56][2.0 ± 1.3]
CFDLQYDPWGALHCI[2.41][1.5 ± 0.4]
CLDLQYDMFGALHCV[3.87][1.9 ± 0.7]
CLDLVYDPWGALHCI[4.04][3.1 ± 1.2]
CWVLEYDMFGALHCR[1.30][1.9 ± 1.5]
CWALEYDMFGYLHCR[0.29][0.72]
CWVLEYDMFGFLHCR[0.072][0.20]
CWVLEYDMFGYLHCR[0.073][0.19]</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:29329326</Reference>
<Target_Name>Avi-tagged interleukin-17A</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>IX104 phage display library(X3CX12CX3)</Library_Name>
<Affinity_Measurement_Method>ELISA,Surface plasmon resonance (SPR)</Affinity_Measurement_Method>
<Affinity_Measurement_Description>BIAcore T200 was used to determine binding affinity and kinetics of the peptides to IL-17A. Avitagged IL-17A was captured to streptavidin sensor chip.For each SPR run, the sensor was first conditioned by 8 cycles of blank prior to sample injections.The resulting sensorgrams of the concentration series of a same peptide were fitted globally to extract binding kinetics and affinity with BIAcore T200 Evaluation Software 2.0 using a 1:1 binding model. Pure peptides from the two libraries were assayed in AlphaLISA format to investigate the potential for disruption of the IL-17A/IL-17RA cytokine-receptor interaction in a biochemical format. In general, the IC50 values determined by AlphaLISA agreed quite closely with the KD values determined through SPR analysis.As was observed in SPR for this family, the differences in AlphaLISA activity between the affinity matured peptides were not significant, with several peptides having IC50's in the 0.2 to 2.0 μMrange.</Affinity_Measurement_Description>
<Brief_Description>IX104 phage display library(X3CX12CX3) consisting of 18 random amino acids were selected against 100 nM of Avi-tagged IL-17A. After three rounds of selection were completed, the eluted phage pool was deconvoluted by filter-lift.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3315</BiopanningDataSetID>
<Peptides>CPDEKHQ[1.63±0.11]
CPDEKHQ[1.65±0.05]
GLPPREIVD[1.62±0.12]
KACPDEKHS[1.63±0.07]
TRNTRT[1.68±0.05]
QESQEPDIHY[1.75±0.08]
GLPPREIVD[1.83±0.04]
IGLEMVFQLI[1.86±0.07]
INVTKLLIQI[1.72±0.03]
QESQEPDIHY[1.65±0.07]
TTRNTRTR[1.72±0.09]
QRNKAAHSVN[1.75±0.04]</Peptides>
<Motif>GYTEDEIV</Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:29304128</Reference>
<Target_Name>Anti-GapC monoclonal antibody (mAb) 1F4</Target_Name>
<Template_Name>Glyceraldehyde-3-phosphate dehydrogenase</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>Twelve clones showed strong, positive  reactions with mAb 1F4. The OD450 of each  peptide binding to mAb was read using a microplate reader at 450 nm.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3316</BiopanningDataSetID>
<Peptides>YSLRSDY(5)[0.59±0.02]
YSLRQDW(3)[0.37±0.01]
YSLRTDW(3)[0.48±0.01]
YSLRQER(3)[0.50±0.01]
YSLRADR(2)[0.39±0.01]
ALSSLRN(2)[0.55±0.02]
HSIRYDF(2)[0.62±0.01]
HSIRVDW(2)[0.35±0.01]
KVWIVPS(2)[0.50±0.01]
KVWLLHS(2)[0.49±0.02]
DWIFPAF(1)[0.43±0.02]</Peptides>
<Motif></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:29301517</Reference>
<Target_Name>Glycoprotein G</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>ELISA plates were coated with the G1 protein and the purified pET32a(+) vector control protein coated with the same concentration. The absorbance of the reaction was determined at 450 nm with an ELISA microplate reader.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>27 specific peptide ligands displaying 11 different amino acid sequences were obtained, and the HSIRYDF and YSLRSDY clone had a higher affinity to G1 protein than the other clones.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3317</BiopanningDataSetID>
<Peptides>IMPHKHRRKLRL(1)[0.50 ± 0.02]
MLTISQRQLSIS(1)[0.48]
RNRTKKQITTQR(1)[0.56 ± 0.01]
RMKMLMMLMRRK(11)[0.52]</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:29517966 </Reference>
<Target_Name>Anti-RhD monoclonal antibody</Target_Name>
<Template_Name>Blood group Rh(D) polypeptide</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>Plates were coated with monoclonal anti-D at 4 °C overnight. Phage clones were added to the antibody-coated wells and incubated for 1 h at room temperature. The primary phage library was used as the negative control The optical density (OD) at 450 nm was subsequently recorded using a microplate reader.</Affinity_Measurement_Description>
<Brief_Description>In the second and third rounds of biopanning, 75 μg/mL and 50 μg/mL anti-D were incubated with 1e11 amplified phages selected in the first biopanning round for enrichment of high affinity binding.  In addition, the bound phages were merely titered but not amplified in the third round.</Brief_Description>
<BiopanningDataSet_Comments>The secondary structure of the synthesised peptide was predicted, based on its amino acid sequence, using PSIPRED (Psi-blast based secondary structure prediction) methods14. The I-TASSER server was employed to predict the three-dimensional structure15. Rasmol, version 2.7.5 (www.RasMol.org) was applied for the visualisation.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3318</BiopanningDataSetID>
<Peptides>IPLLNPGSMQLS(2/26)
SPPWLPVMPVRA(1/26)
WHYNWQDVSDRQ(3/26)
HSYTQTSLWMKV(1/26)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:29852986</Reference>
<Target_Name>Recombinant dengue virus type 2 NS1 protein(DENV2 NS1)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These new peptide-displayed phages or free peptides from phages may have potential applications in dengue diagnosis.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3319</BiopanningDataSetID>
<Peptides>EHDRMHAYYLTR(2/26)</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:29852986</Reference>
<Target_Name>Recombinant dengue virus type 2 NS1 protein(DENV2 NS1)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>These new peptide-displayed phages or free peptides from phages may have potential applications in dengue diagnosis.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3320</BiopanningDataSetID>
<Peptides>CLNSSQPSC(48/58)
CTMSAASHC(5/58)
CRGATPMSC(2/58)
CFPSHNMHC(1/58)
CNHQPSEGC(1/58)
CASPFLCPC(1/58)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:29858055</Reference>
<Target_Name>Astrocyte(AS1)</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>Three rounds against spinal cord in vivo,  and then three additional cycles of in vitro panning were performed for each cell line using the phages within 1e9 TU Phage libraries respectively. In total, genomes were isolated from a collection of 50–58 phages. The three cell  lines are KT5 cells (AS1; astrocytes), 63 cells (M1; proinflammatory microglia), and Ra2 cells (M2; antiinflammatory microglia). This is the AS1 cell line.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3321</BiopanningDataSetID>
<Peptides>CHHSSSARC(13/51)
CNTGSPYEC(3/51)
CQTQNRSAC(3/51)
CANATCPAC(2/51)
CGSKNSAVC(2/51)
CNGGTPNRC(2/51)
CLKLGEKWC(2/51)
CHHRAGVLC(1/51)
CHNETQKMC(1/51)
CRGATPMSC(1/51)
CDLNSDTQC(1/51)
CDNPDRRKC(1/51)
CDDADQSRC(1/51)
CDFPSRGQC(1/51)
CDGHDQSLC(1/51)
CEHSRPMSC(1/51)
CGPMSSKSC(1/51)
CLDLPNAMC(1/51)
CLNSRQPSC(1/51)
CMAPHSRVC(1/51)
CMCNSFTWC(1/51)
CNDSDTYTC(1/51)
CNTDAHRAC(1/51)
CQGERWMQC(1/51)
CQQSMDPAC(1/51)
CSQLPWYSC(1/51)
CSDARSPKC(1/51)
CTHGLTASC(1/51)
CTQSSAMSC(1/51)
CTAKGLQAC(1/51)
CTCNQMAGC(1/51)
CMARYMSAC(0/51)
CPNSTHRNC(0/51)
CTAHDTNSC(0/51)
CDLLHRGAC(0/51)
CDFPKLRPC(0/51)
CEFSKFRSC(0/51)
CGKTSENSC(0/51)
CHDLNGSMC(0/51)
CIASVDSKC(0/51)
CIGNSNTLC(0/51)
CLGRTNGQC(0/51)
CNRSQQPWC(0/51)
CPNMTNQWC(0/51)
CQFSKFRSC(0/51)
CQRATPGHC(0/51)
CRSANIYTC(0/51)
CSNSSLTHC(0/51)
CSPRPTQTC(0/51)
CSWQIGGNC(0/51)
CTTINQKVC(0/51)
CVPNLQGTC(0/51)
CWTDANRDC(0/51)
CYTDANRDC(0/51)
CYPHNTPNC(0/51)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>55</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:29858055</Reference>
<Target_Name>Proinflammatory microglia(MG1)</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>Three rounds against spinal cord in vivo,  and then three additional cycles of in vitro panning were performed for each cell line using the phages within 1e9 TU Phage libraries respectively. In total, genomes were isolated from a collection of 50–58 phages. The three cell  lines are KT5 cells (AS1; astrocytes), 63 cells (M1; proinflammatory microglia), and Ra2 cells (M2; antiinflammatory microglia). This is the M1 cell line.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3322</BiopanningDataSetID>
<Peptides>CNTGSPYEC(8/50)
CHHSSSARC(7/50)
CQTQNRSAC(4/50)
CHHRAGVLC(2/50)
CMARYMSAC(2/50)
CPNSTHRNC(2/50)
CTAHDTNSC(2/50)
CDLLHRGAC(1/50)
CDFPKLRPC(1/50)
CEFSKFRSC(1/50)
CGKTSENSC(1/50)
CHDLNGSMC(1/50)
CIASVDSKC(1/50)
CIGNSNTLC(1/50)
CLGRTNGQC(1/50)
CNRSQQPWC(1/50)
CPNMTNQWC(1/50)
CQFSKFRSC(1/50)
CQRATPGHC(1/50)
CRSANIYTC(1/50)
CSNSSLTHC(1/50)
CSPRPTQTC(1/50)
CSWQIGGNC(1/50)
CTTINQKVC(1/50)
CVPNLQGTC(1/50)
CWTDANRDC(1/50)
CYTDANRDC(1/50)
CYPHNTPNC(1/50)
CHNETQKMC(1/50)
CRGATPMSC(1/50)
CDLNSDTQC(0/50)
CDNPDRRKC(0/50)
CDDADQSRC(0/50)
CDFPSRGQC(0/50)
CDGHDQSLC(0/50)
CEHSRPMSC(0/50)
CGPMSSKSC(0/50)
CLDLPNAMC(0/50)
CLNSRQPSC(0/50)
CMAPHSRVC(0/50)
CMCNSFTWC(0/50)
CNDSDTYTC(0/50)
CNTDAHRAC(0/50)
CQGERWMQC(0/50)
CQQSMDPAC(0/50)
CSQLPWYSC(0/50)
CSDARSPKC(0/50)
CTHGLTASC(0/50)
CTQSSAMSC(0/50)
CTAKGLQAC(0/50)
CTCNQMAGC(0/50)
CANATCPAC(0/50)
CGSKNSAVC(0/50)
CNGGTPNRC(0/50)
CLKLGEKWC(0/50)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>55</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:29858055</Reference>
<Target_Name>Antiinflammatory microglia(MG2)</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>Three rounds against spinal cord in vivo,  and then three additional cycles of in vitro panning were performed for each cell line using the phages within 1e9 TU Phage libraries respectively. In total, genomes were isolated from a collection of 50–58 phages. The three cell  lines are KT5 cells (AS1; astrocytes), 63 cells (M1; proinflammatory microglia), and Ra2 cells (M2; antiinflammatory microglia). This is the M2 cell line.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3323</BiopanningDataSetID>
<Peptides>CHENDVTWC
CHENDVTWC
CPFSDLNNC
CSNFNRYGC
CKDVNTSMC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:29859290</Reference>
<Target_Name>Acinetobacter baumannii 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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>A. baumannii (A.b.48, A.b.50, A.b.55,A.b.56, and A.b.58) were grown in the medium containing human blood, purified phages (1014 plaque-forming unit (PFU)/ml) were incubated with bacteria grown in BTS (approximately 108 colony-forming unit (CFU)/ml) for 1 h incubation at room temperature (RT). Blood biopanning was done for four rounds.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3324</BiopanningDataSetID>
<Peptides>CERSIRTVC
CERSIRTVC
CWPMHTRTC
CWPMHTRTC
CWPMHTRTC
CYPHSQESC
CRGPTAMSC
CNGHTLLSC
CERSIRTVC
CYLTNTTHC</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:29859290</Reference>
<Target_Name>Acinetobacter baumannii 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.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Amplified phages (1014 PFU/ml) were incubated with A. baumannii strains (A.b.48, A.b.50, A.b.55, A.b.56, and A.b.58) that formed biofilm, Biofilm biopanning was performed for three rounds.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>3325</BiopanningDataSetID>
<Peptides>CRHSQMTVTSRL(15,780)
DWSSWVYRDPQT(14,310)
SHCLARQTMLQV(9,570)
DRWVARDPASIF(7,550)
SQDIRTWNGTRS(2,719)
VEPPNSQHSGPC(2,467)
VHWDFRQWWQPS(2,437)
AYYPFVKGRPLP(1,435)
MHPNAGHGSLMR(1,428)
ASSRRPSVGKGF(1,379)
VTTMSGEISQAR(962)
GFPTRFEALSSN(828)
TGSNSPMWDTEV(722)
HVRLTGWQPTWA(306)
QFDYMRPANDTH(298)
SPCTSFPRCVEL(293)
QLATLHKLSGPT(278)</Peptides>
<Motif></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:29875202</Reference>
<Target_Name>CD63 protein fragment containing the second extracellular loop (CD63 LEL)</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>Phages (1e12 plaque-forming units) were incubated with CD63 LEL purified protein for 2 hours, and unbound phages were removed by washing with PBS solution for three times. The bound phages were recovered with glycine-HCl buffer (pH 2.2), followed by neutralization with tris-HCl buffer (pH 8.8). Recovered phages were titered and amplified for subsequent cycles. This process was repeated twice, and the recovered phage clones’ sequences were identified by high-throughput sequencing (Genewiz).</Brief_Description>
<BiopanningDataSet_Comments>One peptide in particular, CP05, enabled direct painting of exosomes with different moieties irrespective of the origin of exosomes.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>