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

0490919 - ÚOCHB 2019 RIV US eng J - Článek v odborném periodiku
Duboué-Dijon, Elise - Delcroix, Pauline - Martinez-Seara, Hector - Hladílková, J. - Coufal, P. - Křížek, T. - Jungwirth, Pavel
Binding of Divalent Cations to Insulin: Capillary Electrophoresis and Molecular Simulations.
Journal of Physical Chemistry B. Roč. 122, č. 21 (2018), s. 5640-5648. ISSN 1520-6106. E-ISSN 1520-5207
Grant CEP: GA ČR(CZ) GA16-01074S
Institucionální podpora: RVO:61388963
Klíčová slova: insulin * electrophoresis * molecular dynamics * calcium
Obor OECD: Physical chemistry
Impakt faktor: 2.923, rok: 2018
https://pubs.acs.org/doi/10.1021/acs.jpcb.7b12097

In 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.
Trvalý link: http://hdl.handle.net/11104/0285033