The Effect of Resveratrol on Binding and Esterase Activity of Human and Rat Albumin


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Abstract

The directional effect on albumin of the molecules which modulate its binding and/or esterase activity could allow stoichiometric and/or catalytic detoxification of organophosphates in the bloodstream. In this study, the effect of polyphenols on binding and catalytic activity of human (HSA) and rat (RSA) serum albumins has been investigated by molecular modeling on the examples of trans-resveratrol and paraoxon. Molecular docking of the paraoxon molecule into the Sudlow II site of HSA and RSA was followed by a calculation of conformational changes and free energies of the albumin-paraoxon complex formation using molecular dynamics simulation. The same calculation was carried out in the presence of a trans-resveratrol molecule in the Sudlow I site. It has been shown that the effect of resveratrol only consists in decreasing pseudo-esterase activity of RSA towards paraoxon.

About the authors

D. A. Belinskaia

Sechenov Institute of Evolutionary Physiology and Biochemistry

Author for correspondence.
Email: d_belinskaya@mail.ru
Russian Federation, St. Petersburg

A. A. Batalova

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: d_belinskaya@mail.ru
Russian Federation, St. Petersburg

N. V. Goncharov

Sechenov Institute of Evolutionary Physiology and Biochemistry; Research Institute of Hygiene

Email: d_belinskaya@mail.ru
Russian Federation, St. Petersburg; St. Petersburg

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