Articles producció científica> Química Física i Inorgànica

Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations

  • Identification data

    Identifier: PC:1924
    Authors:
    Josep M. PobletAlbert Solé-DauraVincent GoovaertsKaren StroobantsGregory AbsillisPablo Jiménez-LozanoJonathan D. HirstTatjana N. Parac-VogtJorge J. Carbó
    Abstract:
    DOI: 10.1002/chem.201602263 URL: http://onlinelibrary.wiley.com/doi/10.1002/chem.201602263/abstract;jsessionid=A78A0F5D7DA73B8D67E1019C41603BD2.f02t02?systemMessage=Due+to+essential+maintenance+the+subscribe%2Frenew+pages+will+be+unavailable+on+Wednesday+26+October+between+02%3A00+-+08%3A00+BST%2F+09%3A00+%E2%80%93+15%3A00++SGT%2F+21%3A00-+03%3A00+EDT.+Apologies+for+the+inconvenience. Filiació URV: SI Inclòs a la memòria: SI
  • Others:

    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
    Link to the original source: http://onlinelibrary.wiley.com/doi/10.1002/chem.201602263/abstract
    Licence document URL: https://repositori.urv.cat/ca/proteccio-de-dades/
    Article's DOI: 10.1002/chem.201602263
    Entity: Universitat Rovira i Virgili
    Journal publication year: 2016
    First page: 15280
    Publication Type: Article Artículo Article
  • Keywords:

    Proteïnes
    Polioxometal·lats
    Dinàmica molecular
    proteins
    polyoxometalates
    molecular dynamics
    Chemistry
    Química
    Química
    1521-3765
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