| GALECKI, K., K. HUNTER, Gabriela DAŇKOVÁ, E. RIVERA, LW TUNG a K. MC SHERRY. Experimental and theoretical investigation of bezafibrate binding to serum albumins. Journal of Luminescence. Amserdam: Elsevier, 2016, roč. 177, September, s. 235-241. ISSN 0022-2313. Dostupné z: https://dx.doi.org/10.1016/j.jlumin.2016.04.052. |
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@article{1380304,
author = {Galecki, K. and Hunter, K. and Daňková, Gabriela and Rivera, E. and Tung, LW and Mc Sherry, K.},
article_location = {Amserdam},
article_number = {September},
doi = {http://dx.doi.org/10.1016/j.jlumin.2016.04.052},
keywords = {Serum albumins; Bezafibrate; Molecular simulation; Fluorescence spectra; Fluorescence lifetime},
language = {eng},
issn = {0022-2313},
journal = {Journal of Luminescence},
title = {Experimental and theoretical investigation of bezafibrate binding to serum albumins},
volume = {177},
year = {2016}
}
TY - JOUR
ID - 1380304
AU - Galecki, K. - Hunter, K. - Daňková, Gabriela - Rivera, E. - Tung, LW - Mc Sherry, K.
PY - 2016
TI - Experimental and theoretical investigation of bezafibrate binding to serum albumins
JF - Journal of Luminescence
VL - 177
IS - September
SP - 235-241
EP - 235-241
PB - Elsevier
SN - 00222313
KW - Serum albumins
KW - Bezafibrate
KW - Molecular simulation
KW - Fluorescence spectra
KW - Fluorescence lifetime
N2 - 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.
ER -
GALECKI, K., K. HUNTER, Gabriela DAŇKOVÁ, E. RIVERA, LW TUNG a K. MC SHERRY. Experimental and theoretical investigation of bezafibrate binding to serum albumins. \textit{Journal of Luminescence}. Amserdam: Elsevier, 2016, roč.~177, September, s.~235-241. ISSN~0022-2313. Dostupné z: https://dx.doi.org/10.1016/j.jlumin.2016.04.052.
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