源自α-淀粉酶抑制剂tendamistat的环肽的生物学和结构特性。

Biological and structural properties of cyclic peptides derived from the alpha-amylase inhibitor tendamistat.

作者信息

Ono S, Hirano T, Yasutake H, Matsumoto T, Yamaura I, Kato T, Morita H, Fujii T, Yamazaki I, Shimasaki C, Yoshimura T

机构信息

Department of Chemical and Biochemical Engineering, Toyama University, Japan.

出版信息

Biosci Biotechnol Biochem. 1998 Aug;62(8):1621-3. doi: 10.1271/bbb.62.1621.

DOI:10.1271/bbb.62.1621

PMID:9757571

Abstract

Six cyclic peptides with 5, 7, 9, 11, 13, and 15 amino acids, with the inhibitory sequence of the alpha-amylase inhibitor tendamistat, were synthesized. The 11-residue peptide inhibited porcine pancreatic alpha-amylase most potently (K1 0.29 +/- 0.09 microM). For the 11-residue peptide, the circular dichroism study suggested a preliminary relationship between its inhibitory activity and structural property.

摘要

合成了六种含有5、7、9、11、13和15个氨基酸的环肽，其具有α-淀粉酶抑制剂tendamistat的抑制序列。11个残基的肽对猪胰α-淀粉酶的抑制作用最强（K1为0.29±0.09微摩尔）。对于11个残基的肽，圆二色性研究表明其抑制活性与结构性质之间存在初步关系。