Author, as appears in the article.: Sole-Daura, Albert; Goovaerts, Vincent; Stroobants, Karen; Absillis, Gregory; Jimenez-Lozano, Pablo; Poblet, Josep M.; Hirst, Jonathan D.; Parac-Vogt, Tatjana N.; Carbo, Jorge J.;
Department: Química Física i Inorgànica
URV's Author/s: Carbó Martin, Jorge Juan / Poblet Rius, Josep Maria
Keywords: Water oxidation catalysts Selective hydrolysis Proteins Polyoxometalates Peptide-bond Peptide hydrolysis Molecular dynamics Keggin anions Human serum-albumin Homogeneous catalyst Egg-white lysozyme Dft calculations Atpase activity Artificial protease Alzheimers-disease polyoxometalates peptide hydrolysis molecular dynamics dft calculations
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.
Thematic Areas: Química Organic chemistry Medicina i Materiais Interdisciplinar General medicine General chemistry Farmacia Engenharias iii Engenharias ii Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Ciências agrárias i Chemistry, multidisciplinary Chemistry (miscellaneous) Chemistry (all) Chemistry Catalysis Biotecnología Biodiversidade Astronomia / física
licence for use: https://creativecommons.org/licenses/by/3.0/es/
Author's mail: josepmaria.poblet@urv.cat j.carbo@urv.cat
Author identifier: 0000-0002-4533-0623 0000-0002-3945-6721
Record's date: 2024-09-07
Papper version: info:eu-repo/semantics/acceptedVersion
Link to the original source: https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/chem.201602263
Licence document URL: https://repositori.urv.cat/ca/proteccio-de-dades/
Papper original source: Chemistry-A European Journal. 22 (43): 15280-15289
APA: Sole-Daura, Albert; Goovaerts, Vincent; Stroobants, Karen; Absillis, Gregory; Jimenez-Lozano, Pablo; Poblet, Josep M.; Hirst, Jonathan D.; Parac-Vogt, (2016). Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations. Chemistry-A European Journal, 22(43), 15280-15289. DOI: 10.1002/chem.201602263
Article's DOI: 10.1002/chem.201602263
Entity: Universitat Rovira i Virgili
Journal publication year: 2016
Publication Type: Journal Publications
Repositori URV