Binding of Divalent Cations to Insulin : Capillary Electrophoresis and Molecular Simulations
(2018) In Journal of Physical Chemistry B 122(21). p.5640-5648- Abstract
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... (More)
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.
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- author
- Duboué-Dijon, Elise ; Delcroix, Pauline ; Martinez-Seara, Hector ; Hladílková, Jana LU ; Coufal, Pavel ; Křížek, Tomáš and Jungwirth, Pavel
- organization
- publishing date
- 2018-05-31
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Physical Chemistry B
- volume
- 122
- issue
- 21
- pages
- 9 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:29360367
- scopus:85047989464
- ISSN
- 1520-6106
- DOI
- 10.1021/acs.jpcb.7b12097
- language
- English
- LU publication?
- yes
- id
- 7b780d7c-dc81-4325-a3c8-ba7515b44a18
- date added to LUP
- 2018-06-12 14:18:47
- date last changed
- 2025-01-08 11:02:41
@article{7b780d7c-dc81-4325-a3c8-ba7515b44a18,
abstract = {{<p>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.</p>}},
author = {{Duboué-Dijon, Elise and Delcroix, Pauline and Martinez-Seara, Hector and Hladílková, Jana and Coufal, Pavel and Křížek, Tomáš and Jungwirth, Pavel}},
issn = {{1520-6106}},
language = {{eng}},
month = {{05}},
number = {{21}},
pages = {{5640--5648}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Physical Chemistry B}},
title = {{Binding of Divalent Cations to Insulin : Capillary Electrophoresis and Molecular Simulations}},
url = {{http://dx.doi.org/10.1021/acs.jpcb.7b12097}},
doi = {{10.1021/acs.jpcb.7b12097}},
volume = {{122}},
year = {{2018}},
}