How Cu(II) binding affects structure and dynamics of α-synuclein revealed by molecular dynamics simulations

Savva, Loizos and Platts, James A. ORCID: https://orcid.org/0000-0002-1008-6595 2023. How Cu(II) binding affects structure and dynamics of α-synuclein revealed by molecular dynamics simulations. Journal of Inorganic Biochemistry 239 , 112068. 10.1016/j.jinorgbio.2022.112068

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Abstract

We report accelerated molecular dynamics simulations of α-Synuclein and its complex with two Cu(II) ions bound to experimentally determined binding sites. Adding two Cu(II) ions, one bound to the N-terminal region and one to the C-terminus, decreases size and flexibility of the peptide while introducing significant new contacts within and between N-terminus and non-Aβ component (NAC). Cu(II) ions also alter the pattern of secondary structure within the peptide, inducing more and longer-lasting elements of secondary structure such as β-strands and hairpins. Free energy surfaces, obtained from reweighting the accelerated molecular dynamics boost potential, further demonstrate the restriction on size and flexibility that results from binding of copper ions.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Advanced Research Computing @ Cardiff (ARCCA) Chemistry
Publisher:	Elsevier
ISSN:	0162-0134
Date of First Compliant Deposit:	2 December 2022
Date of Acceptance:	8 November 2022
Last Modified:	02 Aug 2024 08:32
URI:	https://orca.cardiff.ac.uk/id/eprint/154615

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