RANDOM PEPTIDE LIBRARIES - A SOURCE OF SPECIFIC PROTEIN-BINDING MOLECULES
RANDOM PEPTIDE LIBRARIES - A SOURCE OF SPECIFIC PROTEIN-BINDING MOLECULES
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DOI：
10.1126/science.2143033
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发表时间：
1990-07-27
期刊：
影响因子：
56.9
通讯作者：
DEVLIN, PE
中科院分区：
文献类型：
--
作者：
DEVLIN, JJ;PANGANIBAN, LC;DEVLIN, PE
构建并筛选随机肽序列文库，以鉴定与蛋白质特异性结合的肽。其中之一大约为 2 次。 107 个不同的 15 个残基肽序列在大肠杆菌噬菌体 M13 的表面表达。每个噬菌体编码一个随机序列，并将其表达为与 pIII 的功能复合物，pIII 是一种次要外壳蛋白，每个噬菌体有 5 个分子。从该文库中分离出编码九种不同的链霉亲和素结合肽序列的噬菌体。核心共有序列是 His-Pro-Gln，这些噬菌体与链霉亲和素的结合被生物素抑制。这种类型的文库可以识别与蛋白质（或其他大分子）结合的肽，而这些蛋白质对肽没有已知的亲和力。
Libraries of random peptides sequences were constructed and screened to identify peptides that specifically bind to proteins. In one of these about 2 .times. 107 different 15-residue peptide sequences were expressed on the surface of the coliphage M13. Each phage encoded a single random sequence and expressed it as a function complex with pIII, a minor coat protein present at five molecules per phage. Phage encoding nine different streptavidin-binding peptide sequences were isolated from this library. The core consensus sequence was His-Pro-Gln and binding of these phage to streptavidin was inhibited by biotin. This type of library makes it possible to identify peptides that bind to proteins (or other macromolecules) that have no previously known affinity for peptides.