Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling
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 (<sup>1</sup...
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2021-09-01
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| Series: | International Journal of Molecular Sciences |
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| author | Daria A. Belinskaia Polina A. Voronina Mikhail A. Vovk Vladimir I. Shmurak Anastasia A. Batalova Richard O. Jenkins Nikolay V. Goncharov |
| author_facet | Daria A. Belinskaia Polina A. Voronina Mikhail A. Vovk Vladimir I. Shmurak Anastasia A. Batalova Richard O. Jenkins Nikolay V. Goncharov |
| author_sort | Daria A. Belinskaia |
| collection | DOAJ |
| description | 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 (<sup>1</sup>H NMR) has been applied to the study of true esterase activity of albumin, using the example of bovine serum albumin (BSA) and <i>p</i>-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 <i>p</i>-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. |
| first_indexed | 2024-03-10T06:58:57Z |
| format | Article |
| id | doaj.art-7eada823d59743969689a6e39c58b979 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T06:58:57Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-7eada823d59743969689a6e39c58b9792023-11-22T16:12:20ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-09-0122191059310.3390/ijms221910593Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular ModellingDaria A. Belinskaia0Polina A. Voronina1Mikhail A. Vovk2Vladimir I. Shmurak3Anastasia A. Batalova4Richard O. Jenkins5Nikolay V. Goncharov6Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, RussiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, RussiaCentre for Magnetic Resonance, St. Petersburg State University, Universitetskij pr., 26, Peterhof, 198504 St. Petersburg, RussiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, RussiaSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, RussiaLeicester School of Allied Health Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UKSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, pr. Torez 44, 194223 St. Petersburg, RussiaSerum 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 (<sup>1</sup>H NMR) has been applied to the study of true esterase activity of albumin, using the example of bovine serum albumin (BSA) and <i>p</i>-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 <i>p</i>-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.https://www.mdpi.com/1422-0067/22/19/10593albuminesterases<i>p</i>-nitrophenyl acetate<i>p</i>-nitophenyl propionateNMRmolecular docking |
| spellingShingle | Daria A. Belinskaia Polina A. Voronina Mikhail A. Vovk Vladimir I. Shmurak Anastasia A. Batalova Richard O. Jenkins Nikolay V. Goncharov Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling International Journal of Molecular Sciences albumin esterases <i>p</i>-nitrophenyl acetate <i>p</i>-nitophenyl propionate NMR molecular docking |
| title | Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling |
| title_full | Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling |
| title_fullStr | Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling |
| title_full_unstemmed | Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling |
| title_short | Esterase Activity of Serum Albumin Studied by <sup>1</sup>H NMR Spectroscopy and Molecular Modelling |
| title_sort | esterase activity of serum albumin studied by sup 1 sup h nmr spectroscopy and molecular modelling |
| topic | albumin esterases <i>p</i>-nitrophenyl acetate <i>p</i>-nitophenyl propionate NMR molecular docking |
| url | https://www.mdpi.com/1422-0067/22/19/10593 |
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