Experimental and theoretical investigation of bezafibrate
binding to serum albumins

J 2016

Experimental and theoretical investigation of bezafibrate binding to serum albumins

GALECKI, K., K. HUNTER, Gabriela DAŇKOVÁ, E. RIVERA, LW TUNG et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

30000 3. Medical and Health Sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

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

Abstract

V originále

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.

Citovat

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.

@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 and K. MC SHERRY. Experimental and theoretical investigation of bezafibrate binding to serum albumins. \textit{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.

Detailed Information on Publication Record