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.

Základní údaje

Originální název

Experimental and theoretical investigation of bezafibrate binding to serum albumins

Autoři

GALECKI, K. (616 Polsko), K. HUNTER (826 Velká Británie a Severní Irsko), Gabriela DAŇKOVÁ (203 Česká republika, domácí), E. RIVERA (840 Spojené státy), LW TUNG (344 Hongkong) a K. MC SHERRY (372 Irsko)

Vydání

Journal of Luminescence, Amserdam, Elsevier, 2016, 0022-2313

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

30000 3. Medical and Health Sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.686

Kód RIV

RIV/00216224:14310/16:00094242

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1016/j.jlumin.2016.04.052

UT WoS

000377997700035

Klíčová slova anglicky

Serum albumins; Bezafibrate; Molecular simulation; Fluorescence spectra; Fluorescence lifetime

Štítky

AKR, rivok

Změněno: 11. 5. 2017 15:38, Ing. Andrea Mikešková

Anotace

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 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.

@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.

Podrobný výpis o publikaci