Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation

被引：91

作者：

Liu, Yanqin ^{[1
]}

Carver, John A. ^{[2
]}

Calabrese, Antonio N. ^{[1
]}

Pukala, Tara L. ^{[1
]}

机构：

[1] Univ Adelaide, Sch Chem & Phys, Adelaide, SA 5005, Australia

[2] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2014年 / 1844卷 / 09期

基金：

澳大利亚研究理事会;

关键词：

alpha-Synuclein; Amyloid fibril; Gallic acid; NMR spectroscopy; Ion mobility mass spectrometry; AMYLOID FIBRIL FORMATION; IONIZATION MASS-SPECTROMETRY; B-CRYSTALLIN; NONCOVALENT COMPLEXES; CONFORMATIONAL-CHANGES; PARKINSONS-DISEASE; LEWY BODIES; IN-VITRO; OLIGOMERS; FLAVONOIDS;

D O I：

10.1016/j.bbapap.2014.04.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The accumulation of protein aggregates containing amyloid fibrils, with alpha-synuclein being the main component, is a pathological hallmark of Parkinson's disease (PD). Molecules which prevent the formation of amyloid fibrils or disassociate the toxic aggregates are touted as promising strategies to prevent or treat PD. In the present study, in vitro Thioflavin T fluorescence assays and transmission electron microscopy imaging results showed that gallic acid (GA) potently inhibits the formation of amyloid fibrils by alpha-synuclein. Ion mobility-mass spectrometry demonstrated that GA stabilises the extended, native structure of alpha-synuclein, whilst NMR spectroscopy revealed that GA interacts with alpha-synuclein transiently. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：1481 / 1485

页数：5

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