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Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates

Research Institute of Hygiene, Occupational Pathology and Human Ecology, bld.93 p.o. Kuz’molovsky, Leningrad Region 188663, Russia
Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, St. Petersburg 194223, Russia
School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK
Koltsov Institute of Developmental Biology, Russian Academy of Sciences, 26 Vavilova str., Moscow 119334, Russia
Author to whom correspondence should be addressed.
Molecules 2017, 22(7), 1201;
Received: 4 June 2017 / Revised: 30 June 2017 / Accepted: 12 July 2017 / Published: 18 July 2017
PDF [2282 KB, uploaded 19 July 2017]


The albumin molecule, in contrast to many other plasma proteins, is not covered with a carbohydrate moiety and can bind and transport various molecules of endogenous and exogenous origin. The enzymatic activity of albumin, the existence of which many scientists perceive skeptically, is much less studied. In toxicology, understanding the mechanistic interactions of organophosphates with albumin is a special problem, and its solution could help in the development of new types of antidotes. In the present work, the history of the issue is briefly examined, then our in silico data on the interaction of human serum albumin with soman, as well as comparative in silico data of human and bovine serum albumin activities in relation to paraoxon, are presented. Information is given on the substrate specificity of albumin and we consider the possibility of its affiliation to certain classes in the nomenclature of enzymes. View Full-Text
Keywords: albumin; esterases; organophosphates; docking; molecular modeling albumin; esterases; organophosphates; docking; molecular modeling

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Goncharov, N.V.; Belinskaia, D.A.; Shmurak, V.I.; Terpilowski, M.A.; Jenkins, R.O.; Avdonin, P.V. Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates. Molecules 2017, 22, 1201.

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