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Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations

  • Dades identificatives

    Identificador: PC:1924
    Autors:
    Josep M. PobletAlbert Solé-DauraVincent GoovaertsKaren StroobantsGregory AbsillisPablo Jiménez-LozanoJonathan D. HirstTatjana N. Parac-VogtJorge J. Carbó
    Resum:
    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
  • Altres:

    Autor segons l'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
    Departament: Química Física i Inorgànica
    Autor/s 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
    Paraules clau: proteins polyoxometalates molecular dynamics
    Resum: 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.
    Grup de recerca: Química Quàntica
    Àrees temàtiques: Chemistry Química Química
    Accès a la llicència d'ús: https://creativecommons.org/licenses/by/3.0/es/
    ISSN: 1521-3765
    Identificador de l'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
    Data d'alta del registre: 2016-10-25
    Pàgina final: 15289
    Volum de revista: 22
    Versió de l'article dipositat: info:eu-repo/semantics/acceptedVersion
    Enllaç font original: http://onlinelibrary.wiley.com/doi/10.1002/chem.201602263/abstract
    URL Document de llicència: https://repositori.urv.cat/ca/proteccio-de-dades/
    DOI de l'article: 10.1002/chem.201602263
    Entitat: Universitat Rovira i Virgili
    Any de publicació de la revista: 2016
    Pàgina inicial: 15280
    Tipus de publicació: Article Artículo Article
  • Paraules clau:

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