Takai Eisuke, Uda Ken, Matsushita Shuhei, Shikiya Yui, Yamada Yoichi, Shiraki Kentaro, Zako Tamotsu, Maeda Mizuo
Faculty of Pure and Applied Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305-8573, Japan.
Biotechnol Prog. 2014 Mar-Apr;30(2):470-8. doi: 10.1002/btpr.1866. Epub 2014 Jan 16.
In this article, we discuss the effects of amino acids on amyloid aggregation of lysozyme. l-cysteine (Cys) dramatically inhibited fibrillation of lysozyme, whereas other amino acids (including l-arginine) did not. In the presence of Cys, the aggregation pathway of lysozyme shifted from fibrillation to the formation of the small worm-like aggregates with unfolding. The interaction between Cys and lysozyme was observed to be non-covalent, suggesting that the thiophilic interaction between the thiol group on the side chain of Cys and the core sequence of lysozyme significantly contributes to the inhibition of amyloid aggregation. These findings provide a new basis for the design of a biocompatible additive to prevent amyloid fibrillation.
在本文中，我们讨论了氨基酸对溶菌酶淀粉样聚集的影响。L-半胱氨酸（Cys）显著抑制了溶菌酶的纤维化，而其他氨基酸（包括L-精氨酸）则没有。在Cys存在的情况下，溶菌酶的聚集途径从纤维化转变为形成具有解折叠的小蠕虫状聚集体。观察到Cys与溶菌酶之间的相互作用是非共价的，这表明Cys侧链上的巯基与溶菌酶的核心序列之间的硫亲和相互作用对淀粉样聚集的抑制有显著贡献。这些发现为设计一种生物相容性添加剂以防止淀粉样纤维化提供了新的基础。
