Academic Journal

Esterase Activity of Serum Albumin Studied by 1H NMR Spectroscopy and Molecular Modelling

التفاصيل البيبلوغرافية
العنوان: Esterase Activity of Serum Albumin Studied by 1H NMR Spectroscopy and Molecular Modelling
المؤلفون: Daria A. Belinskaia, Polina A. Voronina, Mikhail A. Vovk, Vladimir I. Shmurak, Anastasia A. Batalova, Richard O. Jenkins, Nikolay V. Goncharov
المصدر: International Journal of Molecular Sciences; Volume 22; Issue 19; Pages: 10593
بيانات النشر: Multidisciplinary Digital Publishing Institute
سنة النشر: 2021
المجموعة: MDPI Open Access Publishing
مصطلحات موضوعية: albumin, esterases, p -nitrophenyl acetate, p -nitophenyl propionate, NMR, molecular docking, molecular dynamics
جغرافية الموضوع: agris
الوصف: 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.
نوع الوثيقة: text
وصف الملف: application/pdf
اللغة: English
Relation: Biochemistry; https://dx.doi.org/10.3390/ijms221910593
DOI: 10.3390/ijms221910593
الاتاحة: https://doi.org/10.3390/ijms221910593
Rights: https://creativecommons.org/licenses/by/4.0/
رقم الانضمام: edsbas.36BEE8E0
قاعدة البيانات: BASE