Peptides binding to a Gb3 mimic selected from a phage library
Peptides binding to a Gb3 mimic selected from a phage library
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DOI：
10.1016/j.bbagen.2004.04.009
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发表时间：
2004-08-04
影响因子：
3
通讯作者：
Kobayashi, K
中科院分区：
文献类型：
--
作者：
Miura, Y;Sasao, Y;Kobayashi, K
从12-mer肽文库中选择与Gb 3模拟物结合的肽。在金表面形成Gb 3模拟物的自组装单分子层（SAM），利用噬菌体展示肽库进行生物淘选。三轮生物淘选后，从10个噬菌体克隆中获得4个单独的序列，并且具有特异性7聚体序列（FHENWPS）的所选肽显示出与RCA一样强的对Gb 3模拟物的亲和力（120）。分子动力学计算表明，多肽与Gb 3模拟物通过疏水相互作用和氢键形成结合，协同作用在识别过程中起重要作用。Stx-1结合被肽抑制。(C)2004 Elsevier B. V.保留所有权利。
Peptides binding to a Gb3 mimic were selected from 12-mer peptide library. The self-assembled monolayer (SAM) of a Gb3 mimic was formed on the gold surface, and biopanning was carried out with the phage display peptide library. After three rounds of biopanning, four individual sequences were obtained from 10 phage clones, and the selected peptides having the specific 7-mer sequence (FHENWPS) showed affinities to the Gb3 mimic as strong as to RCA(120). Molecular dynamics calculations suggested that the peptides bound to the Gb3 mimic by hydrophobic interaction and hydrogen bonding formation, and the cooperative interactions played an important role in the recognition. The Stx-1 binding was inhibited by the peptides. (C) 2004 Elsevier B.V. All rights reserved.