Biological selection of peptides for poly(l-lactide) substrates.
Biological selection of peptides for poly(l-lactide) substrates.
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DOI：
10.1021/la8008442
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发表时间：
2008-05
期刊：
影响因子：
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通讯作者：
H. Matsuno;J. Sekine;H. Yajima;T. Serizawa
中科院分区：
文献类型：
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作者：
H. Matsuno;J. Sekine;H. Yajima;T. Serizawa
从噬菌体展示肽库中鉴定了识别α型聚（L-丙交酯）（PLLA）结晶膜的短肽。酶联免疫吸附试验（ELISA）显示，α形式的PLLA的噬菌体克隆的表观结合常数大于那些的噬菌体文库。α形式PLLA的特异性指数是指结构相似的无规聚（甲基丙烯酸甲酯）（at-PMMA），支持所选噬菌体的α形式PLLA特异性结合。具有质子供体侧基和疏水烷基的氨基酸残基在特定噬菌体克隆上的七肽序列中相对富集，从而表明存在氢键以及PLLA的α形式与肽之间的疏水相互作用。表面等离子体共振（SPR）分析显示，游离的c22七肽（Gln-Leu-Met-His-Asp-Tyr-Arg）与α形式的PLLA的结合常数大于与参照物在-PMMA、无定形PLLA和β形式的PLLA的结合常数。发现c22肽可以识别PLLA多晶型物中的微小差异，例如结晶状态和PLLA官能团的排列。
Short peptides that recognize the alpha form of poly( l-lactide) (PLLA) crystalline films were identified from a phage-displayed peptide library. An enzyme-linked immunosorbent assay (ELISA) revealed that the apparent binding constants of the phage clones for the alpha form of PLLA were greater than those of the unselected phage library. The specificity index for the alpha form of PLLA referred to a structurally similar atactic poly(methyl methacrylate) (at-PMMA), supporting the alpha form of PLLA specific binding of the selected phage. Amino acid residues with proton-donor lateral groups and hydrophobic alkyl groups were relatively enriched in a sequence of heptapeptides on the specific phage clones, thereby suggesting the presence of hydrogen bonding as well as hydrophobic interactions between the alpha form of PLLA and the peptides. Surface plasmon resonance (SPR) analysis revealed that the binding constant of the freed c22 heptapeptide (Gln-Leu-Met-His-Asp-Tyr-Arg) for the alpha form of PLLA was greater than those for reference at-PMMA, amorphous PLLA, and the beta form of PLLA. It was found that c22 peptide can recognize slight differences in PLLA polymorphs such as a crystalline state and an arrangement of PLLA functional groups.