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Binding of Divalent Cations to Insulin: Capillary Electrophoresis and Molecular Simulations

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    SYSNO ASEP0492074
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleBinding of Divalent Cations to Insulin: Capillary Electrophoresis and Molecular Simulations
    Author(s) Dubué-Dijon, E. (FR)
    Delcroix, Pauline (UFCH-W)
    Martinez-Seara, H. (FI)
    Hladílková, J. (SE)
    Coufal, P. (CZ)
    Křížek, T. (CZ)
    Jungwirth, P. (CZ)
    Source TitleJournal of Physical Chemistry B. - : American Chemical Society - ISSN 1520-6106
    Roč. 122, č. 21 (2018), s. 5640-5648
    Number of pages9 s.
    Languageeng - English
    CountryUS - United States
    Keywordsneutron scattering ; secretory granules ; aqueous solutions
    Subject RIVCF - Physical ; Theoretical Chemistry
    OECD categoryPhysical chemistry
    R&D ProjectsGA16-01074S GA ČR - Czech Science Foundation (CSF)
    Method of publishingOpen access
    Institutional supportUFCH-W - RVO:61388955
    UT WOS000434236900038
    EID SCOPUS85047989464
    DOI10.1021/acs.jpcb.7b12097
    AnnotationIn the present study, we characterize the binding of divalent cations to insulin in aqueous salt solutions by means of capillary electrophoresis and molecular dynamics simulations. The results show a strong pH dependence. At low pH, at which all the carboxylate groups are protonated and the protein has an overall positive charge, all the cations exhibit only weak and rather unspecific interactions with insulin. In contrast, at close to neutral pH, when all the carboxylate groups are deprotonated and negatively charged, the charge-neutralizing effect of magnesium, calcium, and zinc, in particular, on the electrophoretic mobility of insulin is significant. This is also reflected in the results of molecular dynamics simulations showing accumulation of cations at the protein surface, which becomes smaller in magnitude upon effective inclusion of electronic polarization via charge rescaling.
    WorkplaceJ. Heyrovsky Institute of Physical Chemistry
    ContactMichaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196
    Year of Publishing2019
Number of the records: 1  

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