Abstract

This study is focused on the characterization of interactions of valinomycin (Val), a macrocyclic dodecadepsipeptide antibiotic ionophore, with rubidium cation, Rb(+). Capillary affinity electrophoresis was employed for the experimental evaluation of the strength of the Val-Rb(+) complex. The study involved the measurement of the change of effective electrophoretic mobility of Val at increasing concentration of Rb(+) cation in the BGE. From the dependence of Val effective electrophoretic mobility on the Rb(+) cation concentration in the BGE (methanolic solution of 100 mM Tris, 50 mM acetic acid, 0-1 mM RbCl), the apparent binding (stability) constant (K(b)) of the Val-Rb(+) complex in methanol was evaluated as log K(b)=4.63+/-0.27. According to the quantum mechanical density functional theory calculations employed to predict the most probable structure of Val-Rb(+) complex, Val is stabilized by strong non-covalent bond interactions of Rb(+) with six ester carbonyl oxygen atoms so that the position of the "central" Rb(+) cation in the Val cage is symmetric.

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