<result><BiopanningDataSet><Item><BiopanningDataSetID>2451</BiopanningDataSetID>
<Peptides>FSVSFPSLPAPPDRS(18)
GRVTYYSCGVSLLFQ(4)
AGPVPLHSLSYYYNQ(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21762809</Reference>
<Target_Name>ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39)</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>f5-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biotinylated unmodified hASL(Lys3) (UUU) and ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39) were attached to streptavidin selection plates. The first round of screening was conducted with the unmodified hASL(Lys3) (UUU), followed by multiple rounds of screening with the triply modified hASL(Lys3)(UUU). Bound phages were eluted from the plates using basic condition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2452</BiopanningDataSetID>
<Peptides>RVTHHAFLGAHRTVG(10)
RAVMTVVWPVSFAGF(5)
PAVASTSSLIIDGPF(2)
PKAFQYGGRAVGGLW(1)
AAHVSEHYVSGSLRP(1)
ASVGPAPWAMTPPVS(1)
APALWYPWRSLLPLY(1)
ASLHPVPKTWFFLLS(1)
WSHSRNTADVPVSML(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21762809</Reference>
<Target_Name>ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39)</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>f5-15mer phage display library (X15)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biotinylated unmodified hASL(Lys3) (UUU) and ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39) were attached to streptavidin selection plates. The first round of screening was conducted with the unmodified hASL(Lys3) (UUU), followed by multiple rounds of screening with the triply modified hASL(Lys3)(UUU). Bound phages were eluted from the plates using acid condition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2453</BiopanningDataSetID>
<Peptides>HRGYCRDRWNCGEYF(8)
PHRQCSAPAKSCKILP(8)
TLPACHELPKHCKRRG(4)
TLPACHELPKHCNEAR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21762809</Reference>
<Target_Name>ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39)</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>f88-4/Cys6 phage display library (X4CX6CX4)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biotinylated unmodified hASL(Lys3) (UUU) and ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39) were attached to streptavidin selection plates. The first round of screening was conducted with the unmodified hASL(Lys3) (UUU), followed by multiple rounds of screening with the triply modified hASL(Lys3)(UUU). Bound phages were eluted from the plates using basic condition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2454</BiopanningDataSetID>
<Peptides>NGPECNAYMVRCRGYH(4)
GNSNCPMLNEQCPWQD(1)
HTETCINIRNTCTTVA(1)
LKLPCKITINNCQLAG(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:21762809</Reference>
<Target_Name>ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39)</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>f88-4/Cys6 phage display library (X4CX6CX4)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biotinylated unmodified hASL(Lys3) (UUU) and ASL(Lys3) (UUU-ms2t6A37;mcm5s2U34;Ψ39) were attached to streptavidin selection plates. The first round of screening was conducted with the unmodified hASL(Lys3) (UUU), followed by multiple rounds of screening with the triply modified hASL(Lys3)(UUU). Bound phages were eluted from the plates using acid condition.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2455</BiopanningDataSetID>
<Peptides>AHSANNFDVKGI
GHSHPTLGWTNG
HIWTGSIWRTWD
HLYHFSSWLYAR
KFLLPNPQAGAP
LSTASTEKSWIN
MPLMSEPALEML
QAHNPNRYMASW
SSLSTYHHRWHL
TPMVERNYNAAD
YFDWGLSNANDT
YSAHNYIGDSGP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:24266517</Reference>
<Target_Name>Anti-DENV E EDIII HuScFv</Target_Name>
<Template_Name>Envelope protein E</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>2456</BiopanningDataSetID>
<Peptides>VSSTQDFP(13)[26.032]
DGSIPWST(8)[28.087]
AFSEAAQT(5)[14.013]
ADAPSNGW(1)[12.007]
DNDNYAFP(1)[2.396]
DYADYSDL(1)[ND]
AADYDPLA(1)[ND]</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:20735141</Reference>
<Target_Name>Human breast carcinoma SKBR-3 (HER positive) 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>f8-8mer phage display library (X8)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of wild type phage and affinity selected phages to SKBR-3 cells was measured by ELISA. The ELISA signal in milliabsorbance units (mAU)/min was determined, reproduced from the graph and shown. The value of wild type phage was 2.996. ND denotes not determined.</Affinity_Measurement_Description>
<Brief_Description>The f8/8 landscape phage library was first incubated with empty culture flask to remove the phages that specifically bound to the culture flask. The resultant depleted library was then used as an input library to the culture flask containing the control MCF-10A cells (HER negative cells). This negative selection was performed to remove phage that binds to the receptors of healthy cells. Then the depleted phage library was transferred to the flask with target SKBR-3 cancer cells (HER positive cells). During each round of affinity selection, after cell-surface-bound phages were eluted, the cells were lysed to release the cell-internalized phages to obtain cell-internalizing peptides. The cell-internalized phages were recovered from cell lysates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2457</BiopanningDataSetID>
<Peptides>DGSIPWST(13)[28.087]
VSSTQDFP(10)[26.032]
DNGSGISW(5)[24.026]
DTKTAPAW(3)[16.117]
GSTDSDLK(2)[12.007]
ATTAPSYP(1)[2.043]
AAATKSDL(1)[2.043]</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:20735141</Reference>
<Target_Name>Human breast carcinoma SKBR-3 (HER positive) 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>f8-8mer phage display library (X8)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of wild type phage and affinity selected phages to SKBR-3 cells was measured by ELISA. The ELISA signal in milliabsorbance units (mAU)/min was determined, reproduced from the graph and shown. The value of wild type phage was 2.996.</Affinity_Measurement_Description>
<Brief_Description>The f8/8 landscape phage library was first incubated with empty culture flask to remove the phages that specifically bound to the culture flask. The resultant depleted library was then used as an input library to the culture flask containing the control MCF-10A cells (HER negative cells). This negative selection was performed to remove phage that binds to the receptors of healthy cells. Then the depleted phage library was transferred to the flask with target SKBR-3 cancer cells (HER positive cells). During each round of affinity selection, cell-surface-bound phages were eluted.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2458</BiopanningDataSetID>
<Peptides>LTHPRWP(2)
TTYNSPP(2)
ARPLEIT(2)
TDRLHFL(2)
HPSRSLD(1)
TFAKSAY(1)
TYSTLGY(1)
EQFSAPI(1)
QHHPTYM(1)
HSHYSLK(1)
MSLSHIT(1)
FTHPRRR(1)
SMYGSYN(1)
SLDALLS(1)
TQLLEPT(1)
ARPRNIT(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>16</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:24659568</Reference>
<Target_Name>Human synovium-derived mesenchymal stem cells, hSMSCs</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In the negative selection procedure, the Ph.D.-7 phage display library was incubated with the fibroblasts for 1 h to exclude the fibroblast affinity phage clones. The supernatant was then collected and incubated with hSMSCs for 1 h to allow hSMSCs internalization. Subsequently, the hSMSCs were washed for 10 min to remove the poorly binding phage clones. The hSMSCs were neutralized with 150 mL of 1 M Tris-HCl (pH 9.1), and lysed in 20% NP-40 for 30 min. The phage clones from the lysed hSMSCs were collected and amplified in Escherichia coli ER2738 (NEB), and then titrated and purified.</Brief_Description>
<BiopanningDataSet_Comments>The identified peptide (LTHPRWP) was designated as an hSMSCs-affinity peptide (L7). PRHLPTW (P7), a randomly scrambled peptide, was used as the negative control, whereas RGD, a peptide consisting of three amino acids (arginine, glycine, and aspartic acid), was used as the positive control. The hSMSCs were incubated for 1 h with FITC-labeled L7, RGD, or P7, and measured via FCM. The average fluorescence intensity was 126.2 ± 13.0 for the hSMSCs incubated with FITC-L7, 118.1 ± 17.3 for the hSMSCs incubated with FITC-RGD, and 5.4 ± 2.2 for the hSMSCs incubated with FITC-P7. To investigate the species specificity of the identified peptide, rat and rabbit SMSCs were also cultured and incubated with FITC-L7, RGD, or P7, and the fluorescent intensities were measured via FCM. This result suggests that L7 has high affinity and specificity for SMSCs and can bind with human, rat, and rabbit SMSCs without species specificity. Thereafter, L7 was covalently conjugated onto both polycaprolactone (PCL) electrospun meshes and human decalcified bone scaffolds (hDBSc) to investigate its TE applications. After 24 h coculture with human SMSCs (hSMSCs), L7-conjugated PCL electrospun meshes had significantly more adherent hSMSCs than the control group, and the cells expanded well. Similar results were obtained using hDBSs. These results suggest that the novel L7 peptide sequence has a high specific affinity to SMSCs. Covalently conjugating this peptide to either artificial polymer material (PCL mesh) or natural material (hDBS) significantly enhances the adhesion of SMSCs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2459</BiopanningDataSetID>
<Peptides>LTHPRWP(3/20)
YSIPKSS(3/20)
SILPYPY(2/20)
TFAKSAY(2/20)
ASLVRMM(2/20)
IVLPYPI(1/20)
HSHYSLK(1/20)
DFKLPAS(1/20)
SETATHP(1/20)
SWHFVVS(1/20)
EQFSAPI(1/20)
VPPSMRP(1/20)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>12</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:24659568</Reference>
<Target_Name>Human synovium-derived mesenchymal stem cells, hSMSCs</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In the negative selection procedure, the Ph.D.-7 phage display library was incubated with the fibroblasts for 1 h to exclude the fibroblast affinity phage clones. The supernatant was then collected and incubated with hSMSCs for 1 h to allow hSMSCs internalization. Subsequently, the hSMSCs were washed for 10 min to remove the poorly binding phage clones. The hSMSCs were neutralized with 150 mL of 1 M Tris-HCl (pH 9.1), and lysed in 20% NP-40 for 30 min. The phage clones from the lysed hSMSCs were collected and amplified in Escherichia coli ER2738 (NEB), and then titrated and purified.</Brief_Description>
<BiopanningDataSet_Comments>Twenty phage clones were randomly selected. An empty phage was found. The identified peptide (LTHPRWP) was designated as an hSMSCs-affinity peptide (L7). PRHLPTW (P7), a randomly scrambled peptide, was used as the negative control, whereas RGD, a peptide consisting of three amino acids (arginine, glycine, and aspartic acid), was used as the positive control. The hSMSCs were incubated for 1 h with FITC-labeled L7, RGD, or P7, and measured via FCM. The average fluorescence intensity was 126.2 ± 13.0 for the hSMSCs incubated with FITC-L7, 118.1 ± 17.3 for the hSMSCs incubated with FITC-RGD, and 5.4 ± 2.2 for the hSMSCs incubated with FITC-P7. To investigate the species specificity of the identified peptide, rat and rabbit SMSCs were also cultured and incubated with FITC-L7, RGD, or P7, and the fluorescent intensities were measured via FCM. This result suggests that L7 has high affinity and specificity for SMSCs and can bind with human, rat, and rabbit SMSCs without species specificity. Thereafter, L7 was covalently conjugated onto both polycaprolactone (PCL) electrospun meshes and human decalcified bone scaffolds (hDBSc) to investigate its TE applications. After 24 h coculture with human SMSCs (hSMSCs), L7-conjugated PCL electrospun meshes had significantly more adherent hSMSCs than the control group, and the cells expanded well. Similar results were obtained using hDBSs. These results suggest that the novel L7 peptide sequence has a high specific affinity to SMSCs. Covalently conjugating this peptide to either artificial polymer material (PCL mesh) or natural material (hDBS) significantly enhances the adhesion of SMSCs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2460</BiopanningDataSetID>
<Peptides>LTHPRWP(11/20)
SILPYPY(2/20)
SHPASHD(1/20)
TFAKSAY(1/20)
TDRLHFL(1/20)
VRPHTSS(1/20)
SAWTYEY(1/20)
DFKLPAS(1/20)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:24659568</Reference>
<Target_Name>Human synovium-derived mesenchymal stem cells, hSMSCs</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In the negative selection procedure, the Ph.D.-7 phage display library was incubated with the fibroblasts for 1 h to exclude the fibroblast affinity phage clones. The supernatant was then collected and incubated with hSMSCs for 1 h to allow hSMSCs internalization. Subsequently, the hSMSCs were washed for 10 min to remove the poorly binding phage clones. The hSMSCs were neutralized with 150 mL of 1 M Tris-HCl (pH 9.1), and lysed in 20% NP-40 for 30 min. The phage clones from the lysed hSMSCs were collected and amplified in Escherichia coli ER2738 (NEB), and then titrated and purified.</Brief_Description>
<BiopanningDataSet_Comments>Twenty phage clones were randomly selected. An empty phage was found. The identified peptide (LTHPRWP) was designated as an hSMSCs-affinity peptide (L7). PRHLPTW (P7), a randomly scrambled peptide, was used as the negative control, whereas RGD, a peptide consisting of three amino acids (arginine, glycine, and aspartic acid), was used as the positive control. The hSMSCs were incubated for 1 h with FITC-labeled L7, RGD, or P7, and measured via FCM. The average fluorescence intensity was 126.2 ± 13.0 for the hSMSCs incubated with FITC-L7, 118.1 ± 17.3 for the hSMSCs incubated with FITC-RGD, and 5.4 ± 2.2 for the hSMSCs incubated with FITC-P7. To investigate the species specificity of the identified peptide, rat and rabbit SMSCs were also cultured and incubated with FITC-L7, RGD, or P7, and the fluorescent intensities were measured via FCM. This result suggests that L7 has high affinity and specificity for SMSCs and can bind with human, rat, and rabbit SMSCs without species specificity. Thereafter, L7 was covalently conjugated onto both polycaprolactone (PCL) electrospun meshes and human decalcified bone scaffolds (hDBSc) to investigate its TE applications. After 24 h coculture with human SMSCs (hSMSCs), L7-conjugated PCL electrospun meshes had significantly more adherent hSMSCs than the control group, and the cells expanded well. Similar results were obtained using hDBSs. These results suggest that the novel L7 peptide sequence has a high specific affinity to SMSCs. Covalently conjugating this peptide to either artificial polymer material (PCL mesh) or natural material (hDBS) significantly enhances the adhesion of SMSCs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2461</BiopanningDataSetID>
<Peptides>CHLGYPGRC[0.656 ± 0.032]
CHYSYPGVC[0.811 ± 0.045]
CHLNYPGYC[0.846 ± 0.152]
CHLRYPGEC[1.087 ± 0.105]
CYKGYPGYC[0.293 ± 0.009]</Peptides>
<Motif>YPG</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:24497417</Reference>
<Target_Name>Anti-Claudin 18.2 monoclonal antibody IMAB362</Target_Name>
<Template_Name>Claudin 18.2</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>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of picked clones to IMAB362 was detected by Phage ELISA. Absorbance at 450 nm was determined. Data shown were reproduced from the graph and expressed as the mean of two experiments ± S.D.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Three of the peptide sequences (CHLGYPGRC, CHYSYPGVC and CHLNYPGYC) were selected for further binding, SAR analysis, and optimization via peptide microarrays.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2462</BiopanningDataSetID>
<Peptides>PRTGTWRSSIAYGGG(17)
PGTGTWRSYLRFGGG(1)
PVTGTWTSSIASWMG(1)
PYTGTWRSSIWVLSG(1)
PGTGTWRSWLSFNVG(1)</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:24356963</Reference>
<Target_Name>Fc region of human immunoglobulin G (IgG)</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>T7 PXTGTWX8G phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The phage library was biopanned against a biotinylated human Fc region (Jackson ImmunoResearch) immobilized on streptavidin MagneSphere@ paramagnetic particles (Promega).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2463</BiopanningDataSetID>
<Peptides>SWDIAWPPLKVP(6)[0.752 ± 0.029]
NILPYNKTMLVK(3)[ND]
SSSNTTTKHVFT(1)[ND]
DSYYTKTERNTH(1)[ND]
YEFPRSWDMETN(1)[ND]
NRPDSAQFWLHH(1)[ND]
GWEVTWPASYAF(1)[ND]</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:24604160</Reference>
<Target_Name>Human glioblastoma cell line A172</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>Specific binding of phage SWDI (displaying SWDIAWPPLKVP) to A172 was evaluated by phage ELISA. Absorbance at 405 nm was determined. The ASNL phage, the random phage from the phage libraries, was used as the control phage. The results represent the mean values ± SEM (standard error of the mean) of two independent experiments analyzed in triplicate. The value shown was reproduced from the graph. The value of the control phage was 0.202 ± 0.024. ND denotes not determined.</Affinity_Measurement_Description>
<Brief_Description>The human embryonic kidney cell line HEK 293 was used for substraction; the human glioblastoma cell line A172 for selection. The entire subtraction/selection cycle was repeated four times.</Brief_Description>
<BiopanningDataSet_Comments>Immunofluorescence staining with anti-M13 phage antibody was performed to observe the specific binding of phage SWDI (displaying SWDIAWPPLKVP) to A172 cells. SWDI phages revealed by the red fluorescent foci were seen on the cell surface of A172; however, no fluorescent signals were present when A172 cells were incubated with the negative control, phage ASNL, which was picked randomly from phage library. Besides, results of ELISA shown that the binding activity of the phage displaying SWDIAWPPLKVP peptide in A172 was more than 10-fold higher than that of the control phage. Then the selected peptide SWDIAWPPLKVP was inserted into adenoviral hexon protein. As a result, the modified Ad5 had increased infectivity in A172 cells, compared with that in control cell lines.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2464</BiopanningDataSetID>
<Peptides>SRPKPPNPS(15)[4.116]
CKRDSISPYSC(6)[9.892]
KTKKPPNPS(4)[5.309]
RLKPPNPTE(2)[4.216]
RKPPNPPPP(1)[4.380]
RRDTISPYS(1)[NT]</Peptides>
<Motif>KPPNP</Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:8855309</Reference>
<Target_Name>IgG from cerebro spinal fluid of multiple sclerosis (MS) patient 1</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>pVIII-9aa and pVIII-9aa.Cys phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description> Average values (A405) from two experiments have been determined. Results are expressed as the ratio between the average value of the tested clone and that of wild-type phage (clone/wt A405). Data shown were reproduced from the graph. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>For each selection, CSF IgGs were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2465</BiopanningDataSetID>
<Peptides>KPKTNQIRP(2)[NT]
KKTGNITPK(1)[6.091]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:8855309</Reference>
<Target_Name>IgG from cerebro spinal fluid of multiple sclerosis (MS) patient 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>pVIII-9aa and pVIII-9aa.Cys phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Average values (A405) from two experiments have been determined. Results are expressed as the ratio between the average value of the tested clone and that of wild-type phage (clone/wt A405). Data shown were reproduced from the graph. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>For each selection, CSF IgGs were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2466</BiopanningDataSetID>
<Peptides>CKRDSISPYSC(6)[10.007, 1.035, 1.234]
CYSATAGPSPC(2)[NT, NT, NT]
CYKSTAGPWGC(1)[NT, NT, NT]
CYGASDGPNAC(1)[NT, NT, NT]
CKRDSIPPTSC(1)[NT, NT, NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:9532590</Reference>
<Target_Name>IgG from the cerebrospinal fluid (CSF) of multiple sclerosis (MS) patients</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>pVIII-9aa.Cys phage display library (CX9C)</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of the selected phagotopes to the CSF1, CSF2 and CSF3 was detected by ELISA on immobilized phage. Average values (A405nm) from two independent experiments have been determined. Results are expressed as the ratio between the average value of the tested phagotope and that of wild type phage (clone/wt A405 nm). Data shown were reproduced from the graph. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>For each selection, 5 microgram of CSF IgG were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2467</BiopanningDataSetID>
<Peptides>FDRLSLADVEQVSIEEAKAWALVQLRDW(11)[2.742, 3.362]
WRTDVRWLSEFEEAEVEGKRPGVWLYGT(9)[6.704, 7.684]
SSRADDVVWVSTGEEAAWRRQWLDLRTV(9)[2.339, 4.168]
ADAVLPWGSSARWDIGGWQVASGGGTQA(5)[24.903, 26.285]
GGGSPVRAEWAQDIRSRSEREMLVWLGK(2)[20.854, 23.347]
AEPGVRERTEMEMGEIFGNLDLCMARRW(1)[13.420, 13.735]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:9762658</Reference>
<Target_Name>IgG from cerebro spinal fluid of multiple sclerosis (MS) patient 1</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>X28 and X28 M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of the selected phagotopes to the CSF and serum IgG from patient 1 was detected by ELISA. For each sample equal amounts of IgG were used and antibody recognition of the tested phagotope and wild type phage was measured. Average values (A405 nm) from two independent experiments have been determined. The background signal obtained on the wild type phage was subtracted. Results are expressed as the ratio between the subtracted value of the tested phagotope obtained by using CSF IgG and that observed using serum IgG (CSF A 405 nm/serum A 405 nm). These data shown were reproduced from the graph. Data obtained by using samples from the same patient at 2 years time interval are also shown.</Affinity_Measurement_Description>
<Brief_Description>For each selection, CSF IgGs were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2468</BiopanningDataSetID>
<Peptides>VPAWRSGGVGTYALLGCDPRISRCTNFS(7)[0.434]
GLWGPPASSRSRPFPPSASVQRQQDVMM(4)[0.176]
SGERARWDWSVFDRVDGLNQGEARIRIG(1)[0.324]
FHPAEPRSRPLADREMCDVRLAVGGVVV(1)[0.166]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>1</Rounds_of_Panning>
<Reference>PMID:9762658</Reference>
<Target_Name>IgG from a mixture of 20 different CSF of multiple sclerosis (MS) patients</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X28 and X28 M13 phage display library pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of IgG from mixtures of 20 MS CSF to crude phage-containing supernatant was detected by ELISA on immobilized phage. For each sample absorbance (405 nm) was measured in two experiments with the phagotope and in two experiments with wild type phage. Data shown were reproduced from the graph.</Affinity_Measurement_Description>
<Brief_Description>For each selection, CSF IgGs were immobilized using magnetic beads coated with goat anti-human IgG Fc-specific Ab.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2469</BiopanningDataSetID>
<Peptides>SRLYSWPDEQYERP[0.46]
SSAYSWPWHDTVD[0.56]
SRAEYWWPDWGFF[0.70]
SRMYWWPNWGSQE[0.42]
SRDTVRKDLLLERE[0.22]
SSWLDGLPLYHEV[0.14]
SSDRGWWWPSWGVSR[NT]
SSMYAWPDSSELEK[NT]
SRFGFYGWPDDQY[NT]
SRDRVYGWPPFEE[NT]
SSAYHWPWVESEW[NT]
SRGYSWPWPDDNA[NT]
SSIYSWPWPSNEN[NT]
SSYSWPWPDFNET[NT]
SSWDGFAWPMHQT[NT]
SSWPWGGFEWPKL[NT]
SSRYWWPDWGSRE[NT]
SSLWWPEWGVYTG[NT]
SSYFWWPDWGSSA[NT]
SRGYWWPDWGSGQ[NT]
SSRLQYWWPDWGP[NT]
MYTWPGSPYLQM[NT]
MYSWPGEHYTVH[NT]
MYSWPGV[NT]
YYGWPSE[NT]
QYTWPWP[NT]</Peptides>
<Motif>Y-[ST]-W-P-W, [YFW]-W-W-P-[DE]-W-G</Motif>
<Unique_Sequence_Number>26</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>Tyrosyl-tRNA synthetase, TyrRS</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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2470</BiopanningDataSetID>
<Peptides>SRDWGFWRLPESMA[0.83]
SRDWGFWRLPNPTE[0.76]
SRDWGFWDWGVDR[0.83]
SREWHFWRDYNPT[0.85]
SRDWSFWDVRDWA[0.70]
SREWGFFDPRFLP[0.74]
SRDWHMFFTGPGQ[0.74]
SRDWHYFHGFPSV[0.78]
SRDWALWHPPLSL[0.74]
SRDWGYWHLGEIV[0.57]
SRDWGYWKVPAPS[0.70]
SREWGFFRMPLHD[0.70]
SRDWGFWNMPPGS[0.58]
SRDWGFWNPIGPL[0.80]
SRDWAFWRGDASG[0.47]
SREWAFFRNWDSV[0.70]
SRCGWAAEVRGVC[0.70]
SSCHWGREVRGLC[0.58]
SSERGSGDRGEKG[0.55]</Peptides>
<Motif>R-[DE]-W-[GA]-[FMY]-[WF]-[DHKNR], C-x-W-x(2)-E-V-R-G-[VL]-C</Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>Proline--tRNA ligase</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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>Biotinylated-target protein and phage were incubated together in solution prior to capturing the target-phage complex on streptavidin-coated paramagnetic particles. Or the target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2471</BiopanningDataSetID>
<Peptides>SSWQGNVLLGNWIS[0.60]
SRPMWMNLVNYVS[1.07]
SSVLCRGFCWTDT[0.89]
SSWQCRGFCWAGE[0.68]
SSPTCRGFCWSTS[0.20]
SSNNAFCRFGCWQ[0.60]
SSAGTTRHEELIP[0.20]
MPPPEPR[0.14]</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:10662687</Reference>
<Target_Name>Alcohol dehydrogenase 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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>For the first round of panning, biotinylated-target protein was bound to streptavidin paramagnetic particles. For the second round of panning, biotinylated-target protein and phage were incubated together in solution prior to capturing the target-phage complex on streptavidin-coated paramagnetic particles. For the third round of panning, the target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2472</BiopanningDataSetID>
<Peptides>SSQTDWRKIFQSL[0.36]
SSSTDWLNVWRQL[0.15]
SSATDWGRVYSIL[0.94]
SSASYAPWPIYFA[0.76]
SSGAFKPWPVYSF[0.36]
SRQVEVFKPWPVY[0.44]
SSSFKPWPIYLGS[0.52]
SSEPFSVWPIYKH[0.44]
SSSVPFAPWPVYA[0.62]
SSTSLPFNRWPIY[0.22]</Peptides>
<Motif>T-D-W-x(2)-[IV]-[FWY]-x-L, [FY]-K-P-W-P-[IV]-Y</Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>β-glucosidase</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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>Biotinylated-target protein and phage were incubated together in solution prior to capturing the target-phage complex on streptavidin-coated paramagnetic particles. Or the target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2473</BiopanningDataSetID>
<Peptides>SRYDNWGWTEKLTK[0.64]
SSMYDEDQWILKLN[0.48]
SSMFDDPSWTMLMR[0.61]
SRYDDWGWVHRLS[0.50]
SSYDDWDWVVRLN[0.66]
SRWEWQEFLDGPL[0.55]
SSVRWWSDDEWRM[0.83]</Peptides>
<Motif>[YF]-D-[DE]-W-x-W-x(2)-[KR]-[LM]</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>Hexokinase-1 and hexokinase-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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>The target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2474</BiopanningDataSetID>
<Peptides>SSEEGRKFRWGWL[0.62]
SSLPEERKLRWGWL[0.77]
SSEDNRKLRWGWL[0.58]
SSDARTCRWCWLG[0.44]
SSWFMDCEWQCFT[0.15]
SRWCGEHDRFCRQA[0.38]
SRTRFCSHDDAFC[0.92]</Peptides>
<Motif>[ED]-x-R-K-[CFL]-R-W-[CG]-W-L, C-x-W-x-C, [FW]-C-x(3)-D-x-F-C</Motif>
<Unique_Sequence_Number>7</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>Glycogen phosphorylase, muscle form</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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>The target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2475</BiopanningDataSetID>
<Peptides>SRLLEVSPGWWQM[0.12]
SSFRELKPGWWSY[0.09]
SSWGDYFNWRDGL[0.09]</Peptides>
<Motif>E-[VL]-x-P-G-W-W-x-[MY]</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3/4</Rounds_of_Panning>
<Reference>PMID:10662687</Reference>
<Target_Name>Carboxypeptidase B</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>Twelve different M13 phage libraries pool</Library_Name>
<Affinity_Measurement_Method>ELISA</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Absorbance at 405 nm was measured.</Affinity_Measurement_Description>
<Brief_Description>The target protein was biotinylated and captured on streptavidin-coated 96-well plates.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>