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Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling. / Belinskaia, Daria A.; Voronina, Polina A.; Vovk, Mikhail A.; Shmurak, Vladimir I.; Batalova, Anastasia A.; Jenkins, Richard O.; Goncharov, Nikolay V.

In: International Journal of Molecular Sciences, Vol. 22, No. 19, 10593, 30.09.2021.

Research output: Contribution to journalArticlepeer-review

Harvard

Belinskaia, DA, Voronina, PA, Vovk, MA, Shmurak, VI, Batalova, AA, Jenkins, RO & Goncharov, NV 2021, 'Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling', International Journal of Molecular Sciences, vol. 22, no. 19, 10593. https://doi.org/10.3390/ijms221910593

APA

Belinskaia, D. A., Voronina, P. A., Vovk, M. A., Shmurak, V. I., Batalova, A. A., Jenkins, R. O., & Goncharov, N. V. (2021). Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling. International Journal of Molecular Sciences, 22(19), [10593]. https://doi.org/10.3390/ijms221910593

Vancouver

Belinskaia DA, Voronina PA, Vovk MA, Shmurak VI, Batalova AA, Jenkins RO et al. Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling. International Journal of Molecular Sciences. 2021 Sep 30;22(19). 10593. https://doi.org/10.3390/ijms221910593

Author

Belinskaia, Daria A. ; Voronina, Polina A. ; Vovk, Mikhail A. ; Shmurak, Vladimir I. ; Batalova, Anastasia A. ; Jenkins, Richard O. ; Goncharov, Nikolay V. / Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling. In: International Journal of Molecular Sciences. 2021 ; Vol. 22, No. 19.

BibTeX

@article{c1e5ddbfb4334d0da7ffb32ccd35fb2a,
title = "Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling",
abstract = "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 (1H 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.",
keywords = "Albumin, Esterases, Molecular docking, Molecular dynamics, NMR, P-nitophenyl propionate, P-nitrophenyl acetate",
author = "Belinskaia, {Daria A.} and Voronina, {Polina A.} and Vovk, {Mikhail A.} and Shmurak, {Vladimir I.} and Batalova, {Anastasia A.} and Jenkins, {Richard O.} and Goncharov, {Nikolay V.}",
note = "Belinskaia, D.A.; Voronina, P.A.; Vovk, M.A.; Shmurak, V.I.; Batalova, A.A.; Jenkins, R.O.; Goncharov, N.V. Esterase Activity of Serum Albumin Studied by 1H NMR Spectroscopy and Molecular Modelling. Int. J. Mol. Sci. 2021, 22, 10593. https://doi.org/10.3390/ijms221910593",
year = "2021",
month = sep,
day = "30",
doi = "10.3390/ijms221910593",
language = "English",
volume = "22",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "19",

}

RIS

TY - JOUR

T1 - Esterase activity of serum albumin studied by1h nmr spectroscopy and molecular modelling

AU - Belinskaia, Daria A.

AU - Voronina, Polina A.

AU - Vovk, Mikhail A.

AU - Shmurak, Vladimir I.

AU - Batalova, Anastasia A.

AU - Jenkins, Richard O.

AU - Goncharov, Nikolay V.

N1 - Belinskaia, D.A.; Voronina, P.A.; Vovk, M.A.; Shmurak, V.I.; Batalova, A.A.; Jenkins, R.O.; Goncharov, N.V. Esterase Activity of Serum Albumin Studied by 1H NMR Spectroscopy and Molecular Modelling. Int. J. Mol. Sci. 2021, 22, 10593. https://doi.org/10.3390/ijms221910593

PY - 2021/9/30

Y1 - 2021/9/30

N2 - 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 (1H 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.

AB - 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 (1H 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.

KW - Albumin

KW - Esterases

KW - Molecular docking

KW - Molecular dynamics

KW - NMR

KW - P-nitophenyl propionate

KW - P-nitrophenyl acetate

UR - http://www.scopus.com/inward/record.url?scp=85116040958&partnerID=8YFLogxK

U2 - 10.3390/ijms221910593

DO - 10.3390/ijms221910593

M3 - Article

AN - SCOPUS:85116040958

VL - 22

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 19

M1 - 10593

ER -

ID: 86499850