Probing the inhibitory potency of epigallocatechin gallate against human γB-crystallin aggregation: Spectroscopic, microscopic and simulation studies

被引:13
作者
Chaudhury, Susmitnarayan [1 ,3 ]
Dutta, Anirudha [2 ,4 ]
Bag, Sudipta [1 ]
Biswas, Pranandita [1 ]
Das, Amit Kumar [2 ]
Dasgupta, Swagata [1 ]
机构
[1] Indian Inst Technol Kharagpur, Dept Chem, Kharagpur 721302, W Bengal, India
[2] Indian Inst Technol Kharagpur, Dept Biotechnol, Kharagpur 721302, W Bengal, India
[3] Natl Ctr Biol Sci, Bangalore 560065, Karnataka, India
[4] State Univ New Jersey, Oral Biol Dept, Newark, NJ 07103 USA
关键词
Cataract; Inhibition of aggregation/fibrillation; Epigallocatechin gallate; Spectroscopy; Microscopy; Molecular dynamics simulation; MOLECULAR-DYNAMICS; AMYLOID FIBRILS; S-CRYSTALLIN; GREEN TEA; IN-VITRO; PROTEIN; CATARACT; BINDING; MUTANT; LENS;
D O I
10.1016/j.saa.2017.11.036
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Aggregation of human ocular lens proteins, the crystallins is believed to be one of the key reasons for age-onset cataract. Previous studies have shown that human gamma D-crystallin forms amyloid like fibres under conditions of low pH and elevated temperature. In this article, we have investigated the aggregation propensity of human gamma B-crystallin in absence and presence of epigallocatechin gallate (EGCG), in vitro, when exposed to stressful conditions. We have used different spectroscopic and microscopic techniques to elucidate the inhibitory effect of EGCG towards aggregation. The experimental results have been substantiated by molecular dynamics simulation studies. We have shown that EGCG possesses inhibitory potency against the aggregation of human gamma B-crystallin at low pH and elevated temperature. (C) 2017 Elsevier B.V. All rights reserved.
引用
收藏
页码:318 / 327
页数:10
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