Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/84492
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation |
Other Titles: | Gallic acid interacts with alpha-synuclein to prevent the structural collapse necessary for its aggregation |
Author: | Liu, Y. Carver, J. Calabrese, A. Pukala, T. |
Citation: | BBA: Proteins and Proteomics, 2014; 1844(9):1481-1485 |
Publisher: | Elsevier B.V. |
Issue Date: | 2014 |
ISSN: | 1878-1454 1878-1454 |
Statement of Responsibility: | Yanqin Liu, John A. Carver, Antonio N. Calabrese, Tara L. Pukala |
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: | α-Synuclein; Amyloid fibril; Gallic acid; NMR spectroscopy; Ion mobility mass spectrometry |
Rights: | Copyright © 2014 Elsevier B.V. |
DOI: | 10.1016/j.bbapap.2014.04.013 |
Grant ID: | http://purl.org/au-research/grants/arc/DP1093143 |
Published version: | http://dx.doi.org/10.1016/j.bbapap.2014.04.013 |
Appears in Collections: | Aurora harvest 2 Chemistry and Physics publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.