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首页> 外文期刊>Journal of Molecular Biology >TENDAMISTAT AS A SCAFFOLD FOR CONFORMATIONALLY CONSTRAINED PHAGE PEPTIDE LIBRARIES
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TENDAMISTAT AS A SCAFFOLD FOR CONFORMATIONALLY CONSTRAINED PHAGE PEPTIDE LIBRARIES

机译：Tendamistat作为构象约束噬菌体肽库的支架

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摘要

The alpha-amylase inhibitor Tendamistat (Hoe-467), a 74 amino acid beta-sheet protein from Streptomyces tendae has been expressed on the surface of the filamentous bacteriophage M13. Phage displaying Tendamistat inhibit the hydrolysis of starch by alpha-amylase, indicating that the displayed protein is functional. The displayed Tendamistat has been used as a molecular scaffold for the presentation of constrained random peptides. Two loops, comprising residues 38 to 40 and 60 to 65 of Tendamistat, were randomized using PCR mutagenesis. Libraries of similar to 10(8) different mutant Tendamistat molecules were tested for binding to monoclonal antibody A8, which recognizes endothelin. After three cycles of biopanning, phage were isolated that specifically bound the monoclonal antibody Loop swapping and alanine replacement mutagenesis indicated that residues in the 60 to 65 loop are responsible for binding to the monoclonal antibody. This work demonstrates the use of relatively small non-antibody protein scaffolds for the presentation of constrained random peptide sequences to select for novel binding molecules. [References: 49]
机译：α-淀粉酶抑制剂Tendamistat（Hoe-467）是一种来自腱链霉菌的74个氨基酸的β-折叠蛋白，已在丝状噬菌体M13的表面表达。展示Tendamistat的噬菌体可抑制α-淀粉酶对淀粉的水解，表明所展示的蛋白质具有功能。展示的Tendamistat已被用作分子支架，用于展示受约束的随机肽。使用PCR诱变将包含Tendamistat残基38至40和60至65的两个环随机化。测试了与10（8）个不同的Tendamistat突变体分子相似的文库与识别内皮素的单克隆抗体A8的结合。经过三轮生物淘选后，分离出特异性结合单克隆抗体的噬菌体。环交换和丙氨酸替代诱变表明60至65环中的残基负责与单克隆抗体的结合。这项工作证明了使用相对较小的非抗体蛋白支架来展示受约束的随机肽序列以选择新的结合分子。 [参考：49]

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