Esterase Activity of Serum Albumin Studied by 1H NMR Spectroscopy and Molecular Modelling

被引：16

作者：

Belinskaia, Daria A. ^{[1
]}

Voronina, Polina A. ^{[1
]}

Vovk, Mikhail A. ^{[2
]}

Shmurak, Vladimir, I ^{[1
]}

Batalova, Anastasia A. ^{[1
]}

Jenkins, Richard O. ^{[3
]}

Goncharov, Nikolay, V ^{[1
]}

机构：

[1] Russian Acad Sci, Sechenov Inst Evolutionary Physiol & Biochem, Pr Torez 44, St Petersburg 194223, Russia

[2] St Petersburg State Univ, Ctr Magnet Resonance, Univ Skij Pr 26, St Petersburg 198504, Russia

[3] De Montfort Univ, Leicester Sch Allied Hlth Sci, Leicester LE1 9BH, Leics, England

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2021年 / 22卷 / 19期

关键词：

albumin; esterases; p-nitrophenyl acetate; p-nitophenyl propionate; NMR; molecular docking; molecular dynamics; COMMERCIAL HUMAN ALBUMIN; REDOX STATE; OXIDATION; BINDING; PROTEIN; BOVINE; ORGANOPHOSPHORUS; DETOXICATION; CHEMISTRY; EFFICIENT;

D O I：

10.3390/ijms221910593

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Serum albumin possesses esterase and pseudo-esterase activities towards a number of endogenous and exogenous substrates, but the mechanism of interaction of various esters and other compounds with albumin is still unclear. In the present study, proton nuclear magnetic resonance (H-1 NMR) has been applied to the study of true esterase activity of albumin, using the example of bovine serum albumin (BSA) and p-nitrophenyl acetate (NPA). The site of BSA esterase activity was then determined using molecular modelling methods. According to the data obtained, the accumulation of acetate in the presence of BSA in the reaction mixture is much more intense as compared with the spontaneous hydrolysis of NPA, which indicates true esterase activity of albumin towards NPA. Similar results were obtained for p-nitophenyl propionate (NPP) as substrate. The rate of acetate and propionate release confirms the assumption that there is a site of true esterase activity in the albumin molecule, which is different from the site of the pseudo-esterase activity Sudlow II. The results of molecular modelling of BSA and NPA interaction make it possible to postulate that Sudlow site I is the site of true esterase activity of albumin.Y

引用

页数：22

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