Cysteine inhibits amyloid fibrillation of lysozyme and directs the formation of small worm-like aggregates through non-covalent interactions
作者： Eisuke Takai , Ken Uda , Shuhei Matsushita , Yui Shikiya , Yoichi Yamada
DOI: 10.1002/BTPR.1866
关键词:
摘要: In this article, we discuss the effects of amino acids on amyloid aggregation lysozyme. l-cysteine (Cys) dramatically inhibited fibrillation lysozyme, whereas other (including l-arginine) did not. presence Cys, pathway lysozyme shifted from to formation small worm-like aggregates with unfolding. The interaction between Cys and was observed be non-covalent, suggesting that thiophilic thiol group side chain core sequence significantly contributes inhibition aggregation. These findings provide a new basis for design biocompatible additive prevent fibrillation. © 2014 American Institute Chemical Engineers Biotechnol. Prog., 30:470–478,
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