Toward a molecular mechanism for the interaction of ATP with alpha-synuclein-Reference-Cited by-同舟云学术

Toward a molecular mechanism for the interaction of ATP with alpha-synuclein

Published:2023 Issue:36 Volume:14 Page:9933-9942
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Kamski-Hennekam Evelyn Rose¹,Huang Jinfeng¹,Ahmed Rashik²,Melacini Giuseppe¹²^ORCID

Affiliation:

1. Department of Chemistry and Chemical Biology, McMaster University, Hamilton, ON, L8S 4M1, Canada

2. Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, L8S 4M1, Canada

Abstract

We propose a mechanism for the hydrotrope-like function of ATP on alpha-synuclein whereby ATP enhances initial αS aggregation and inhibits fibril formation in a phosphate-dependent manner that is modulated by PD-related αS mutations E46K and A53T.

Funder

Natural Sciences and Engineering Research Council of Canada

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/SC/D3SC03612J

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5. ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues

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