A-type dimeric epigallocatechin-3-gallate (EGCG) is a more potent inhibitor against the formation of insulin amyloid fibril than EGCG monomer
A-type dimeric epigallocatechin-3-gallate (EGCG) is a more potent inhibitor against the formation of insulin amyloid fibril than EGCG monomer
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A 型二聚体表没食子儿茶素-3-没食子酸酯 (EGCG) 比 EGCG 单体更有效地抑制胰岛素淀粉样原纤维的形成
DOI：
10.1016/j.biochi.2016.03.011
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发表时间：
2016-06-01
期刊：
影响因子：
3.9
通讯作者：
Li, Chun-mei
中科院分区：
文献类型：
--
作者：
Nie, Rong-zu;Zhu, Wei;Li, Chun-mei
由于纤维蛋白聚集体被认为与许多疾病如阿尔茨海默病、糖尿病和帕金森病密切相关，因此越来越多的兴趣和研究集中在寻找潜在的纤颤抑制剂上。在本研究中，表没食子儿茶素没食子酸酯（EGCG）和A型二聚体表没食子儿茶素没食子酸酯（A-type dimmer epigallocatechin-3-gallate）的抑制作用，采用硫代黄素-T（ThT）荧光法、1-苯胺基萘-8-磺酸（ANS）荧光法、动态光散射（DLS）、透射电镜（TEM）、透射电镜（TEM）、傅里叶变换红外（FTIR）光谱和圆二色性（CD）光谱。我们的研究结果证实，A型EGCG二聚体是一个更有效的抑制剂对牛胰岛素淀粉样纤维的形成比EGCG。此外，A型表没食子儿茶素没食子酸酯二聚体不仅能抑制胰岛素淀粉样纤维的形成，而且能改变胰岛素的聚集途径，诱导胰岛素形成无定形聚集体。本研究结果可能为寻找新型抗淀粉样蛋白生成药物提供新的指导。(C)2016 Elsevier B. V.和法国生物化学与生物分子学会（SFBBM）。All rights reserved.
Because fibrillary protein aggregates is regarded to be closely associated with many diseases such as Alzheimer's disease, diabetes, and Parkinson's disease, growing interest and researches have been focused on finding potential fibrillation inhibitors. In the present study, the inhibitory effects of epigallocatechin-3-gallate (EGCG) and A-type dimeric epigallocatechin-3-gallate (A-type EGCG dimer) on the formation of insulin fibrillation were compared by multi-dimensional approaches including thioflavin-T (ThT) fluorescence assay, 1-anilinonaphthalene-8-sulfonic (ANS) fluorescence assay, dynamic light scattering (DLS), transmission electron microscopy (TEM), Fourier transform infrared (FTIR) spectroscopy and circular dichroism (CD) spectroscopy. Our results confirmed that A-type EGCG dimer is a more potent inhibitor against the formation of bovine insulin amyloid fibril than EGCG. In addition, A type EGCG dimer could not only inhibit insulin amyloid fibril formation, but also change the aggregation pathway and induce bovine insulin into amorphous aggregates. The results of the present study may provide a new guide on finding novel anti-amyloidogenic agents. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.