Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates
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 stu...
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| Format: | Article |
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MDPI AG
2017-07-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/22/7/1201 |
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| author | Nikolay V. Goncharov Daria A. Belinskaia Vladimir I. Shmurak Maxim A. Terpilowski Richard O. Jenkins Pavel V. Avdonin |
| author_facet | Nikolay V. Goncharov Daria A. Belinskaia Vladimir I. Shmurak Maxim A. Terpilowski Richard O. Jenkins Pavel V. Avdonin |
| author_sort | Nikolay V. Goncharov |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T21:51:16Z |
| format | Article |
| id | doaj.art-41fe6ddf887a439689238ac69be8240a |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-12T21:51:16Z |
| publishDate | 2017-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-41fe6ddf887a439689238ac69be8240a2022-12-22T00:10:46ZengMDPI AGMolecules1420-30492017-07-01227120110.3390/molecules22071201molecules22071201Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with OrganophosphatesNikolay V. Goncharov0Daria A. Belinskaia1Vladimir I. Shmurak2Maxim A. Terpilowski3Richard O. Jenkins4Pavel V. Avdonin5Research Institute of Hygiene, Occupational Pathology and Human Ecology, bld.93 p.o. Kuz’molovsky, Leningrad Region 188663, RussiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, St. Petersburg 194223, RussiaResearch Institute of Hygiene, Occupational Pathology and Human Ecology, bld.93 p.o. Kuz’molovsky, Leningrad Region 188663, RussiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, St. Petersburg 194223, RussiaSchool of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UKKoltsov Institute of Developmental Biology, Russian Academy of Sciences, 26 Vavilova str., Moscow 119334, RussiaThe 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.https://www.mdpi.com/1420-3049/22/7/1201albuminesterasesorganophosphatesdockingmolecular modeling |
| spellingShingle | Nikolay V. Goncharov Daria A. Belinskaia Vladimir I. Shmurak Maxim A. Terpilowski Richard O. Jenkins Pavel V. Avdonin Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates Molecules albumin esterases organophosphates docking molecular modeling |
| title | Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates |
| title_full | Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates |
| title_fullStr | Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates |
| title_full_unstemmed | Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates |
| title_short | Serum Albumin Binding and Esterase Activity: Mechanistic Interactions with Organophosphates |
| title_sort | serum albumin binding and esterase activity mechanistic interactions with organophosphates |
| topic | albumin esterases organophosphates docking molecular modeling |
| url | https://www.mdpi.com/1420-3049/22/7/1201 |
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