Yonezawa A, Sugiura Y
Institute for Chemical Research, Kyoto University, Japan.
Nucleic Acids Symp Ser. 1992(27):161-2.
In this study, we present a model compound for antiparallel beta-sheet-DNA interaction. Tachyplesin I, cationic antimicrobial peptide, interacts through contacts with the minor groove. Secondary structure of tachyplesin I, antiparallel beta-sheet constrained by two disulfide bridges and connected by beta-turn, contributes significantly to its DNA binding. The present results give valuable information for design of sequence-specific DNA binding peptide based on antiparallel beta-sheet.
在本研究中，我们展示了一种用于反平行β-折叠与DNA相互作用的模型化合物。鲎素I，一种阳离子抗菌肽，通过与小沟的接触进行相互作用。鲎素I的二级结构，由两个二硫键约束并通过β-转角连接的反平行β-折叠，对其与DNA的结合有显著贡献。目前的结果为基于反平行β-折叠设计序列特异性DNA结合肽提供了有价值的信息。
