Replica exchange molecular dynamics simulation of the coordination of Pt(ii)-Phenanthroline to amyloid-β†

Turner, Matthew, Mutter, Shaun T., Kennedy-Britten, Oliver D. and Platts, James A. ORCID: https://orcid.org/0000-0002-1008-6595 2019. Replica exchange molecular dynamics simulation of the coordination of Pt(ii)-Phenanthroline to amyloid-β†. RSC Advances 9 (60) , pp. 35089-35097. 10.1039/C9RA04637B

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Abstract

We report replica exchange molecular dynamics (REMD) simulations of the complex formed between amyloid-β peptides and platinum bound to a phenanthroline ligand, Pt(phen). After construction of an AMBER-style forcefield for the Pt complex, REMD simulation employing temperatures between 270 and 615 K was used to provide thorough sampling of the conformational freedom available to the peptide. We find that the full length peptide Aβ42, in particular, frequently adopts a compact conformation with a large proportion of α- and 3,10-helix content, with smaller amounts of β-strand in the C-terminal region of the peptide. Helical structures are more prevalent than in the metal-free peptide, while turn and strand conformations are markedly less common. Non-covalent interactions, including salt-bridges, hydrogen bonds, and π-stacking between aromatic residues and the phenanthroline ligand, are common, and markedly different from those seen in the amyloid-β peptides alone.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Advanced Research Computing @ Cardiff (ARCCA) Chemistry
Publisher:	Royal Society of Chemistry
ISSN:	2046-2069
Funders:	EPSRC
Date of First Compliant Deposit:	5 November 2019
Date of Acceptance:	24 October 2019
Last Modified:	05 Aug 2024 14:52
URI:	https://orca.cardiff.ac.uk/id/eprint/126592

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