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Probing Polyoxometalate-Protein Interactions Using Molecular Dynamics Simulations

  • Datos identificativos

    Identificador: imarina:5130354
    Autores:
    Sole-Daura, AlbertGoovaerts, VincentStroobants, KarenAbsillis, GregoryJimenez-Lozano, PabloPoblet, Josep M.Hirst, Jonathan D.Parac-Vogt, Tatjana N.Carbo, Jorge J.
    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.
  • Otros:

    Autor según el artículo: 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.;
    Departamento: Química Física i Inorgànica
    Autor/es de la URV: Carbó Martin, Jorge Juan / Poblet Rius, Josep Maria
    Palabras clave: 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
    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.
    Áreas temáticas: 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
    Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
    Direcció de correo del autor: josepmaria.poblet@urv.cat j.carbo@urv.cat
    Identificador del autor: 0000-0002-4533-0623 0000-0002-3945-6721
    Fecha de alta del registro: 2024-09-07
    Versión del articulo depositado: info:eu-repo/semantics/acceptedVersion
    Enlace a la fuente original: https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/chem.201602263
    URL Documento de licencia: https://repositori.urv.cat/ca/proteccio-de-dades/
    Referencia al articulo segun fuente origial: Chemistry-A European Journal. 22 (43): 15280-15289
    Referencia de l'ítem segons les normes 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
    DOI del artículo: 10.1002/chem.201602263
    Entidad: Universitat Rovira i Virgili
    Año de publicación de la revista: 2016
    Tipo de publicación: Journal Publications
  • Palabras clave:

    Catalysis,Chemistry,Chemistry (Miscellaneous),Chemistry, Multidisciplinary,Organic Chemistry
    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
    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
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