Research output: Contribution to journal › Article › peer-review
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 journal › Article › peer-review
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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