Author, as appears in the article.: Josep M. Poblet; Albert Solé-Daura; Vincent Goovaerts; Karen Stroobants; Gregory Absillis; Pablo Jiménez-Lozano; Jonathan D. Hirst; Tatjana N. Parac-Vogt; Jorge J. Carbó
Department: Química Física i Inorgànica
URV's Author/s: POBLET RIUS, JOSEP MARIA; Albert Solé-Daura; Vincent Goovaerts; Karen Stroobants; Gregory Absillis; Pablo Jiménez-Lozano; Jonathan D. Hirst; Tatjana N. Parac-Vogt; CARBÓ MARTIN, JORGE JUAN
Keywords: proteins polyoxometalates molecular dynamics
Abstract: The molecular interactions between the CeIV-substituted Keggin anion [PW11O39Ce(OH2)4]3− (CeK) and hen egg-white lysozyme (HEWL) were investigated by molecular dynamics simulations. The analysis of CeK was compared with the CeIV-substituted Keggin dimer [(PW11O39)2Ce]10− (CeK2) and the ZrIV-substituted Lindqvist anion [W5O18Zr(OH2)(OH)]3− (ZrL) to understand how POM features such as shape, size, charge, or type of incorporated metal ion influence the POM⋅⋅⋅protein interactions. Simulations revealed two regions of the protein in which the CeK anion interacts strongly: cationic sites formed by Arg21 and by Arg45 and Arg68. The POMs chiefly interact with the side chains of the positively charged (arginines, lysines) and the polar uncharged residues (tyrosines, serines, aspargines) via electrostatic attraction and hydrogen bonding with the oxygen atoms of the POM framework. The CeK anion shows higher protein affinity than the CeK2 and ZrL anions, because it is less hydrophilic and it has the right size and shape for establishing interactions with several residues simultaneously. The larger, more negatively charged CeK2 anion has a high solvent-accessible surface, which is sub-optimal for the interaction, while the smaller ZrL anion is highly hydrophilic and cannot efficiently interact with several residues simultaneously.
Research group: Química Quàntica
Thematic Areas: Chemistry Química Química
licence for use: https://creativecommons.org/licenses/by/3.0/es/
ISSN: 1521-3765
Author identifier: 0000-0002-4533-0623; n/a; n/a; n/a; n/a; n/a; 0000-0002-2726-0983; 0000-0002-6188-3957; 0000-0002-3945-6721
Record's date: 2016-10-25
Last page: 15289
Journal volume: 22
Papper version: info:eu-repo/semantics/acceptedVersion
Licence document URL: https://repositori.urv.cat/ca/proteccio-de-dades/
Entity: Universitat Rovira i Virgili
Journal publication year: 2016
First page: 15280
Publication Type: Article Artículo Article
Repositori URV