Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537544 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2014 | 5 Pages |
Abstract
The accumulation of protein aggregates containing amyloid fibrils, with α-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 α-synuclein. Ion mobility-mass spectrometry demonstrated that GA stabilises the extended, native structure of α-synuclein, whilst NMR spectroscopy revealed that GA interacts with α-synuclein transiently.
Keywords
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Yanqin Liu, John A. Carver, Antonio N. Calabrese, Tara L. Pukala,