How oxidized EGCG remodels α-synuclein fibrils into non-toxic aggregates: insights from computational simulations-Reference-Cited by-同舟云学术

How oxidized EGCG remodels α-synuclein fibrils into non-toxic aggregates: insights from computational simulations

Published:2023 Issue:28 Volume:25 Page:19182-19194
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Gonçalves Priscila Baltazar¹^ORCID,Palhano Fernando L.²^ORCID,Cordeiro Yraima¹^ORCID,Sodero Ana Carolina Rennó¹

Affiliation:

1. Faculdade de Farmácia, Programa de Pós-Graduação em Ciências Farmacêuticas, Universidade Federal do Rio de Janeiro, RJ, 21941-902, Brazil

2. Instituto de Bioquímica Médica Leopoldo de Meis, Programa de Biologia Estrutural, Universidade Federal do Rio de Janeiro, Brazil

Abstract

Oxidized EGCG binds to the same α-syn sites as ThT, leading to fibril remodeling. Oxidized EGCG forms H-bonds with non-specific residues while it moves within the fibril core, while ThT binding is dominantly driven by aromatic π-stacking interactions.

Funder

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D3CP02261G

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1. Epidemiology of Parkinson’s disease