Standard

Modulation of Albumin Esterase Activity by Warfarin and Diazepam. / Belinskaia, Daria A.; Batalova, Anastasia A.; Voronina, Polina A.; Shmurak, Vladimir I.; Вовк, Михаил Андреевич; Поляничко, Александр Михайлович; Sych, Tomash S.; Samodurova, Kamila V.; Antonova, Vasilisa K.; Volkova, Anastasia A.; Gerda, Bogdan A.; Jenkins, Richard O.; Goncharov, Nikolay V.

в: International Journal of Molecular Sciences, Том 25, № 21, 11543, 27.10.2024.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Belinskaia, DA, Batalova, AA, Voronina, PA, Shmurak, VI, Вовк, МА, Поляничко, АМ, Sych, TS, Samodurova, KV, Antonova, VK, Volkova, AA, Gerda, BA, Jenkins, RO & Goncharov, NV 2024, 'Modulation of Albumin Esterase Activity by Warfarin and Diazepam', International Journal of Molecular Sciences, Том. 25, № 21, 11543. https://doi.org/10.3390/ijms252111543

APA

Belinskaia, D. A., Batalova, A. A., Voronina, P. A., Shmurak, V. I., Вовк, М. А., Поляничко, А. М., Sych, T. S., Samodurova, K. V., Antonova, V. K., Volkova, A. A., Gerda, B. A., Jenkins, R. O., & Goncharov, N. V. (2024). Modulation of Albumin Esterase Activity by Warfarin and Diazepam. International Journal of Molecular Sciences, 25(21), [11543]. https://doi.org/10.3390/ijms252111543

Vancouver

Belinskaia DA, Batalova AA, Voronina PA, Shmurak VI, Вовк МА, Поляничко АМ и пр. Modulation of Albumin Esterase Activity by Warfarin and Diazepam. International Journal of Molecular Sciences. 2024 Окт. 27;25(21). 11543. https://doi.org/10.3390/ijms252111543

Author

Belinskaia, Daria A. ; Batalova, Anastasia A. ; Voronina, Polina A. ; Shmurak, Vladimir I. ; Вовк, Михаил Андреевич ; Поляничко, Александр Михайлович ; Sych, Tomash S. ; Samodurova, Kamila V. ; Antonova, Vasilisa K. ; Volkova, Anastasia A. ; Gerda, Bogdan A. ; Jenkins, Richard O. ; Goncharov, Nikolay V. / Modulation of Albumin Esterase Activity by Warfarin and Diazepam. в: International Journal of Molecular Sciences. 2024 ; Том 25, № 21.

BibTeX

@article{18348c78cfab4887bebad01f5e15d447,
title = "Modulation of Albumin Esterase Activity by Warfarin and Diazepam",
abstract = "Data are accumulating on the hydrolytic activity of serum albumin towards esters and organophosphates. Previously, with the help of the technology of proton nuclear magnetic resonance (1H NMR) spectroscopy, we observed the yield of acetate in the solution of bovine serum albumin and p-nitrophenyl acetate (NPA). Thus, we showed that albumin possesses true esterase activity towards NPA. Then, using the methods of molecular docking and molecular dynamics, we established site Sudlow I as the catalytic center of true esterase activity of albumin. In the present work, to expand our understanding of the molecular mechanisms of albumin pseudoesterase and true esterase activity, we investigated—in experiments in vitro and in silico—the interaction of anticoagulant warfarin (WRF, specific ligand of site Sudlow I) and benzodiazepine diazepam (DIA, specific ligand of site Sudlow II) with albumins of different species, and determined how the binding of WRF and DIA affects the hydrolysis of NPA by albumin. It was found that the characteristics of the binding modes of WRF in site Sudlow I and DIA in site Sudlow II of human (HSA), bovine (BSA), and rat (RSA) albumins have species differences, which are more pronounced for site Sudlow I compared to site Sudlow II, and less pronounced between HSA and RSA compared to BSA. WRF competitively inhibits true esterase activity of site Sudlow I towards NPA and does not affect the functioning of site Sudlow II. Diazepam can slow down true esterase activity of site Sudlow I in noncompetitive manner. It was concluded that site Sudlow I is more receptive to allosteric modulation compared to site Sudlow II.",
keywords = "albumin, esterases, p-nitrophenyl acetate, inhibitory analysis, NMR, spectrophotometry, molecular modeling, NMR, albumin, esterases, inhibitory analysis, molecular modeling, p-nitrophenyl acetate, spectrophotometry",
author = "Belinskaia, {Daria A.} and Batalova, {Anastasia A.} and Voronina, {Polina A.} and Shmurak, {Vladimir I.} and Вовк, {Михаил Андреевич} and Поляничко, {Александр Михайлович} and Sych, {Tomash S.} and Samodurova, {Kamila V.} and Antonova, {Vasilisa K.} and Volkova, {Anastasia A.} and Gerda, {Bogdan A.} and Jenkins, {Richard O.} and Goncharov, {Nikolay V.}",
year = "2024",
month = oct,
day = "27",
doi = "10.3390/ijms252111543",
language = "English",
volume = "25",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "21",

}

RIS

TY - JOUR

T1 - Modulation of Albumin Esterase Activity by Warfarin and Diazepam

AU - Belinskaia, Daria A.

AU - Batalova, Anastasia A.

AU - Voronina, Polina A.

AU - Shmurak, Vladimir I.

AU - Вовк, Михаил Андреевич

AU - Поляничко, Александр Михайлович

AU - Sych, Tomash S.

AU - Samodurova, Kamila V.

AU - Antonova, Vasilisa K.

AU - Volkova, Anastasia A.

AU - Gerda, Bogdan A.

AU - Jenkins, Richard O.

AU - Goncharov, Nikolay V.

PY - 2024/10/27

Y1 - 2024/10/27

N2 - Data are accumulating on the hydrolytic activity of serum albumin towards esters and organophosphates. Previously, with the help of the technology of proton nuclear magnetic resonance (1H NMR) spectroscopy, we observed the yield of acetate in the solution of bovine serum albumin and p-nitrophenyl acetate (NPA). Thus, we showed that albumin possesses true esterase activity towards NPA. Then, using the methods of molecular docking and molecular dynamics, we established site Sudlow I as the catalytic center of true esterase activity of albumin. In the present work, to expand our understanding of the molecular mechanisms of albumin pseudoesterase and true esterase activity, we investigated—in experiments in vitro and in silico—the interaction of anticoagulant warfarin (WRF, specific ligand of site Sudlow I) and benzodiazepine diazepam (DIA, specific ligand of site Sudlow II) with albumins of different species, and determined how the binding of WRF and DIA affects the hydrolysis of NPA by albumin. It was found that the characteristics of the binding modes of WRF in site Sudlow I and DIA in site Sudlow II of human (HSA), bovine (BSA), and rat (RSA) albumins have species differences, which are more pronounced for site Sudlow I compared to site Sudlow II, and less pronounced between HSA and RSA compared to BSA. WRF competitively inhibits true esterase activity of site Sudlow I towards NPA and does not affect the functioning of site Sudlow II. Diazepam can slow down true esterase activity of site Sudlow I in noncompetitive manner. It was concluded that site Sudlow I is more receptive to allosteric modulation compared to site Sudlow II.

AB - Data are accumulating on the hydrolytic activity of serum albumin towards esters and organophosphates. Previously, with the help of the technology of proton nuclear magnetic resonance (1H NMR) spectroscopy, we observed the yield of acetate in the solution of bovine serum albumin and p-nitrophenyl acetate (NPA). Thus, we showed that albumin possesses true esterase activity towards NPA. Then, using the methods of molecular docking and molecular dynamics, we established site Sudlow I as the catalytic center of true esterase activity of albumin. In the present work, to expand our understanding of the molecular mechanisms of albumin pseudoesterase and true esterase activity, we investigated—in experiments in vitro and in silico—the interaction of anticoagulant warfarin (WRF, specific ligand of site Sudlow I) and benzodiazepine diazepam (DIA, specific ligand of site Sudlow II) with albumins of different species, and determined how the binding of WRF and DIA affects the hydrolysis of NPA by albumin. It was found that the characteristics of the binding modes of WRF in site Sudlow I and DIA in site Sudlow II of human (HSA), bovine (BSA), and rat (RSA) albumins have species differences, which are more pronounced for site Sudlow I compared to site Sudlow II, and less pronounced between HSA and RSA compared to BSA. WRF competitively inhibits true esterase activity of site Sudlow I towards NPA and does not affect the functioning of site Sudlow II. Diazepam can slow down true esterase activity of site Sudlow I in noncompetitive manner. It was concluded that site Sudlow I is more receptive to allosteric modulation compared to site Sudlow II.

KW - albumin

KW - esterases

KW - p-nitrophenyl acetate

KW - inhibitory analysis

KW - NMR

KW - spectrophotometry

KW - molecular modeling

KW - NMR

KW - albumin

KW - esterases

KW - inhibitory analysis

KW - molecular modeling

KW - p-nitrophenyl acetate

KW - spectrophotometry

UR - https://www.mendeley.com/catalogue/1708483b-a5f0-37d5-b7de-34053b924c28/

U2 - 10.3390/ijms252111543

DO - 10.3390/ijms252111543

M3 - Article

VL - 25

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 21

M1 - 11543

ER -

ID: 126558699