Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils

Archives of Biochemistry and Biophysics
Wen-Bo YuPing Zhou

Abstract

The aggregation of alpha-synuclein (AS) is pivotally implicated in the development of Parkinson's disease (PD), inhibiting this process might be effective in treating PD. Here, by using circular dichroism spectroscopy, thioflavin T fluorescence, and atomic force microscopy, we found that trehalose at low concentration disaggregates preformed A53T AS protofibrils and fibrils into small aggregates or even random coil structure, while trehalose at high concentration slows down the structural transition into β-sheet structure and completely prevents the formation of mature A53T AS fibrils. Further work in vivo will be needed to evaluate its potential as a novel strategy for treating PD.

Citations

Dec 10, 2013·Acta Neuropathologica Communications·Darius Ebrahimi-FakhariLara Wahlster
Apr 29, 2014·Biochimica Et Biophysica Acta·Luc BoussetFederica Migliardo
Jun 19, 2012·Neurochemical Research·Dan-Mei LanJian Wang
Dec 17, 2014·Microbiology·Dorota Kuczyńska-WiśnikEwa Laskowska
Jul 14, 2017·Physical Chemistry Chemical Physics : PCCP·Nidhi Katyal, Shashank Deep
Aug 9, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Juan ZhaoPing Zhou
Feb 16, 2019·British Journal of Pharmacology·Masoomeh KhalifehAmirhossein Sahebkar
Jun 3, 2016·Chembiochem : a European Journal of Chemical Biology·Alessandro SinopoliEnrico Rizzarelli
Jun 11, 2020·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Masoomeh KhalifehAmirhossein Sahebkar
Nov 24, 2017·Applied Microbiology and Biotechnology·Kamil PiwowarekIwona Ścibisz
Sep 30, 2018·Nature Communications·Noah Guy Lewis GuibersonJacqueline Burré
Jul 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Kamil PiwowarekSylwia Bonin

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