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含三个半胱氨酸残基的合成寡肽的金属结合与解毒作用

Metal-binding and detoxification effect of synthetic oligopeptides containing three cysteinyl residues.

作者信息

Yoshida A, Kaplan B E, Kimura M

出版信息

Proc Natl Acad Sci U S A. 1979 Jan;76(1):486-90. doi: 10.1073/pnas.76.1.486.

Abstract

Metallothionein is a naturally occurring metal-binding protein with high cysteine content. Oligopeptides containing three cysteinyl residues and having amino acid sequences analogous to portions of this protein were synthesized by the solid-phase method. Strong affinity of the synthetic peptides to Cd2+ and Zn2+ was observed, and the dissociation constants of the peptide-metal complexes were 2-4 orders of magnitude lower than those of cysteine-metal and dithioerythritol-metal complexes. Effectiveness of detoxification of the peptides against Cd toxicity was demonstrated by the higher survival rates of mice treated with the peptides and by the neutralization of Cd toxicity by the peptides in tissue cultures.

摘要

金属硫蛋白是一种天然存在的、富含半胱氨酸的金属结合蛋白。通过固相法合成了含有三个半胱氨酰残基且氨基酸序列与该蛋白部分序列类似的寡肽。观察到合成肽对Cd2+和Zn2+具有很强的亲和力,且肽-金属复合物的解离常数比半胱氨酸-金属和二硫苏糖醇-金属复合物的解离常数低2至4个数量级。用这些肽处理的小鼠存活率更高,以及这些肽在组织培养中对Cd毒性的中和作用,都证明了这些肽对Cd毒性的解毒效果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ad9/382966/8505662799dd/pnas00001-0496-a.jpg

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