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

Yanqin Liu; John A. Carver; Antonio N. Calabrese; Tara L. Pukala

doi:10.1016/j.bbapap.2014.04.013

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

Yanqin Liu, John A. Carver, Antonio N. Calabrese, Tara L. Pukala^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

92 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1481-1485
Number of pages	5
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1844
Issue number	9
DOIs	https://doi.org/10.1016/j.bbapap.2014.04.013
Publication status	Published - Sept 2014

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

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 = "Amyloid fibril, Gallic acid, Ion mobility mass spectrometry, NMR spectroscopy, α-Synuclein",

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AB - 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.

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JO - Biochimica et Biophysica Acta - Proteins and Proteomics

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

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