Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates

• Published in: Molecules (Basel, Switzerland) Switzerland), 2017-07, Vol.22 (7), p.1201
• Main Authors: Goncharov, Nikolay V, Belinskaia, Daria A, Shmurak, Vladimir I, Terpilowski, Maxim A, Jenkins, Richard O, Avdonin, Pavel V
• Format: Article
• Language: English
• Subjects: albumin; Animals; Antidotes; Binding sites; Bovine serum albumin; Carbohydrates; Cattle; docking; Enzymatic activity; Enzyme Activation - drug effects; Enzymes; Esterase; esterases; Esterases - chemistry; Esterases - metabolism; Fatty acids; Human serum albumin; Humans; Hydrolysis; Ligands; Mammals; Models, Molecular; Molecular Conformation; molecular modeling; Organophosphates; Organophosphates - chemistry; Organophosphates - pharmacology; Paraoxon; Plasma proteins; Protein Binding; Proteins; Serum albumin; Serum Albumin - chemistry; Serum Albumin - metabolism; Software packages; Substrate Specificity; Toxicology
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules22071201

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.