Autor según el artículo: 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

Departamento: Química Física i Inorgànica

Autor/es de la URV: 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

Palabras clave: proteins polyoxometalates molecular dynamics

Resumen: 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.

Grupo de investigación: Química Quàntica

Áreas temáticas: Chemistry Química Química

Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/

ISSN: 1521-3765

Identificador del autor: 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

Fecha de alta del registro: 2016-10-25

Página final: 15289

Volumen de revista: 22

Versión del articulo depositado: info:eu-repo/semantics/acceptedVersion

Enlace a la fuente original: http://onlinelibrary.wiley.com/doi/10.1002/chem.201602263/abstract

DOI del artículo: 10.1002/chem.201602263

Entidad: Universitat Rovira i Virgili

Año de publicación de la revista: 2016

Página inicial: 15280

Tipo de publicación: Article Artículo Article