Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer
Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer
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DOI：
10.1039/a708046h
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发表时间：
1998-01-01
期刊：
影响因子：
--
通讯作者：
Mosbach, K
中科院分区：
文献类型：
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作者：
Berglund, J;Lindbladh, C;Mosbach, K
用分子印迹法制备了α（2）-肾上腺素受体模拟物，从噬菌体展示六肽库中筛选出对育亨宾印迹聚合物具有亲和性的噬菌体，用酶免疫分析法测定了噬菌体的亲和性，筛选出的噬菌体库对育亨宾印迹聚合物的亲和性比原始噬菌体库高3倍，从所选文库中鉴定的90个噬菌体克隆中有82个对聚合物表现出低亲和力，这些低结合噬菌体克隆中的8个上的六肽主要由疏水性氨基酸残基组成，并且4个克隆是相同的，8个高亲和力噬菌体克隆中的5个上的六肽含有带正电荷的氨基酸，相同的六肽在这五个克隆中的四个上表达。该研究的结果表明，大多数选择的六肽与聚合物框架形成疏水和/或离子相互作用，而不是仅与育亨宾印迹位点的特异性相互作用。此外，在六肽序列亲和力和它们所含的带正电荷的氨基酸残基的数目之间可以看到直接的相关性。
alpha(2)-Adrenoreceptor mimics, prepared by molecular imprinting of yohimbine, were used to select ligands from a phage display hexapeptide library, Phages with affinity for the yohimbine imprinted methacrylic acid-ethylene glycol dimethacrylate copolymer were selected, Phage affinities were estimated using an enzyme immunoassay, The selected library showed three-fold higher affinity for the imprinted polymer compared with the primary library, Eighty-two of ninety characterized phage clones from the selected library showed low affinity for the polymer, The hexapeptides on eight of these low binding phage clones consisted of mainly hydrophobic amino acid residues, and four clones were identical, The hexapeptides on five of the eight high affinity phage clones contained positively charged amino acids, identical hexapeptides were expressed on four of these five clones, The results of this study suggest that the majority of the selected phages form hydrophobic and/or ionic interactions with the polymer framework rather than specific interactions only with the yohimbine imprinted sites, Furthermore, a direct correlation can be seen between hexapeptide sequence affinity and the number of positively charged amino acid residues they contain.