Esterase activity of serum albumin studied by 1H NMR spectroscopy and molecular modelling

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dc.cclicenceCC-BYen
dc.contributor.authorBELINSKAIA, D.A.
dc.contributor.authorVORONINA, P.A.
dc.contributor.authorVOVK, M.A.
dc.contributor.authorSHMURAK, V.I.
dc.contributor.authorBATALOVA, A.A.
dc.contributor.authorJenkins, R. O.
dc.contributor.authorGONCHAROV, N.V.
dc.date.acceptance2021-09-27
dc.date.accessioned2022-05-24T13:20:19Z
dc.date.available2022-05-24T13:20:19Z
dc.date.issued2021-09-30
dc.descriptionThe Publisher's final version can be found by following the DOI link. Open access article.en
dc.description.abstractSerum 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.en
dc.funderOther external funder (please detail below)en
dc.funder.otherSechenov Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences research program AAAA-A18-118012290142-9en
dc.identifier.citationBELINSKAIA DA, VORONINA PA, VOVK MA, SHMURAK VI, BATALOVA AA, JENKINS RO and GONCHAROV NV. (2021) Esterase activity of serum albumin studied by 1H NMR spectroscopy and molecular modelling. International Journal of Molecular Sciences, 22(19), 10593.en
dc.identifier.doihttps://doi.org/10.3390/ijms221910593
dc.identifier.issn1422-0067
dc.identifier.urihttps://hdl.handle.net/2086/21911
dc.language.isoenen
dc.peerreviewedYesen
dc.projectidAAAA-A18-118012290142-9en
dc.publisherMDPIen
dc.researchinstituteInstitute for Allied Health Sciences Researchen
dc.subjectalbuminen
dc.subjectesterasesen
dc.subjectp-nitrophenyl acetateen
dc.subjectNMRen
dc.subjectmolecular dockingen
dc.subjectmolecular dynamicsen
dc.titleEsterase activity of serum albumin studied by 1H NMR spectroscopy and molecular modellingen
dc.typeArticleen

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