Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide

Turner, Matthew, Mutter, Shaun, Deeth, Robert J. and Platts, James ORCID: https://orcid.org/0000-0002-1008-6595 2018. Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide. PLoS ONE 13 (3) , -. 10.1371/journal.pone.0193668

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Abstract

We report microsecond timescale molecular dynamics simulation of the complex formed between Pt(II)-phenanthroline and the 16 N-terminal residues of the Aβ peptide that is implicated in the onset of Alzheimer's disease, along with equivalent simulations of the metalfree peptide. Simulations from a variety of starting points reach equilibrium within 100 ns, as judged by root mean square deviation and radius of gyration. Platinum-bound peptides deviate rather more from starting points, and adopt structures with larger radius of gyration, than their metal-free counterparts. Residues bound directly to Pt show smaller fluctuation, but others actually move more in the Pt-bound peptide. Hydrogen bonding within the peptide is disrupted by binding of Pt, whereas the presence of salt-bridges are enhanced.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Advanced Research Computing @ Cardiff (ARCCA)
Publisher:	Public Library of Science
ISSN:	1932-6203
Funders:	Engineering and Physical Sciences Research Council
Date of First Compliant Deposit:	27 March 2018
Date of Acceptance:	15 February 2018
Last Modified:	21 Jul 2024 18:12
URI:	https://orca.cardiff.ac.uk/id/eprint/110255

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