Experimental and theoretical investigation of bezafibrate binding to serum albumins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F16%3A00094242" target="_blank" >RIV/00216224:14310/16:00094242 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.jlumin.2016.04.052" target="_blank" >http://dx.doi.org/10.1016/j.jlumin.2016.04.052</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jlumin.2016.04.052" target="_blank" >10.1016/j.jlumin.2016.04.052</a>

Result language
angličtina
Original language name
Experimental and theoretical investigation of bezafibrate binding to serum albumins
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FP - Other medical fields
OECD FORD branch
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Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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