GALECKI, K., K. HUNTER, Gabriela DAŇKOVÁ, E. RIVERA, LW TUNG and K. MC SHERRY. Experimental and theoretical investigation of bezafibrate binding to serum albumins. Journal of Luminescence. Amserdam: Elsevier, 2016, vol. 177, September, p. 235-241. ISSN 0022-2313. Available from: https://dx.doi.org/10.1016/j.jlumin.2016.04.052.
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Basic information
Original name Experimental and theoretical investigation of bezafibrate binding to serum albumins
Authors GALECKI, K. (616 Poland), K. HUNTER (826 United Kingdom of Great Britain and Northern Ireland), Gabriela DAŇKOVÁ (203 Czech Republic, belonging to the institution), E. RIVERA (840 United States of America), LW TUNG (344 Hong Kong) and K. MC SHERRY (372 Ireland).
Edition Journal of Luminescence, Amserdam, Elsevier, 2016, 0022-2313.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 30000 3. Medical and Health Sciences
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 2.686
RIV identification code RIV/00216224:14310/16:00094242
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1016/j.jlumin.2016.04.052
UT WoS 000377997700035
Keywords in English Serum albumins; Bezafibrate; Molecular simulation; Fluorescence spectra; Fluorescence lifetime
Tags AKR, rivok
Changed by Changed by: Ing. Andrea Mikešková, učo 137293. Changed: 11/5/2017 15:38.
Abstract
The purpose of this investigation was to provide insight into the possible mechanism of the intermolecular interactions between antilipemic agent bezafibrate and serum albumins (SAs) including human (HSA) and bovine (BSA). The aim was to indicate the most probable sight of these interactions. Both experimental (spectroscopic) and theoretical methods were applied. It was determined that bezafibrate binds to SAs in one specific binding site, the fatty acid binding site 6. The results obtained from the steady-state and time-resolved fluorescence experiments suggested that existing two distinct stable conformations of the proteins with different exposure to the quencher. The dominate conformer of HSA and BSA characterized by the Stern-Volmer quenching constant (from ratio F-0/F) equal to 1.24.10(4) and 8.48.10(3) M-1 at 298 K, respectively. The docking results and calculated thermodynamics parameters may be suggested that the binding process is spontaneous and might involve van der Waals and hydrogen bonding forces. (c) 2016 Elsevier B.V. All rights reserved.
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