Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18470%2F10%3A00003037" target="_blank" >RIV/62690094:18470/10:00003037 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin
Original language description
Hydroxycinnamic acids (HCAs) possess numerous biological and due to these properties are widely used in folk medicine. Nevertheless, they can interact with protein molecules and cause some structural and functional changes. The possibility of HCAs binding to bovine serum albumin (BSA) under physiological conditions was investigated by the UV-VIS absorption spectroscopy, fluorescence quenching method, and FRET method. The binding constants, number of binding sites and free energy changes were determined.The binding affinities of HCAs were ranked in the order: chlorogenic acid > sinapic acid >= caffeic acid > ferulic acid > o-coumaric acid > p-coumaric acid >= m-coumaric acid, which was confirmed by spectral overlaps of BSA emission spectrum with absorption spectrum of HCA. All free energy changes possessed negative sign indicating the spontaneity of HCA-BSA interaction.
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
CE - Biochemistry
OECD FORD branch
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Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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