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Protein‐ion Interactions: Simulations of Bovine Serum Albumin in Physiological Solutions of NaCl, KCl and LiCl
Author(s) -
Becconi Olga,
Ahlstrand Emma,
Salis Andrea,
Friedman Ran
Publication year - 2017
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201600119
Subject(s) - chemistry , bovine serum albumin , ion , salt (chemistry) , potentiometric titration , electrolyte , molecular dynamics , molecule , inorganic chemistry , computational chemistry , chromatography , organic chemistry , electrode
Specific interactions that depend on the nature of electrolytes are observed when proteins and other molecules are studied by potentiometric, spectroscopic and theoretical methods at high salt concentrations. More recently, it became clear that such interactions may also be observed in solutions that can be described by the Debye‐Hückel theory, i.e., at physiological (0.1 mol dm −3 ) and lower concentrations. We carried out molecular dynamics simulations of bovine serum albumin in physiological solutions at T=300 and 350 K. Analysis of the simulations revealed some differences between LiCl solutions and those of NaCl and KCl. The binding of Li + ions to the protein was associated with a negative free energy of interaction whereas much fewer Na + and K + ions were associated with the protein surface. Interestingly, unlike other proteins BSA does not show a preference to Na + over K + . Quantum chemical calculations identified a significant contribution from polarisation to the hydration of Li + and (to a lesser degree) Na + , which may indicate that polarisable force‐fields will provide more accurate results for such systems.