Study on the interactions of trans-resveratrol and curcumin with bovine α-lactalbumin by spectroscopic analysis and molecular docking

Materials Science & Engineering. C, Materials for Biological Applications
Fakhrossadat Mohammadi, Marzieh Moeeni

Abstract

The ability of bovine α-lactalbumin (BLA) as a whey protein to carry curcumin and trans-resveratrol as two natural polyphenolic compounds was investigated by fluorescence quenching measurements and docking studies. Curcumin is the bioactive component of turmeric and trans-resveratrol is abundant in different types of fruits and vegetables. The binding parameters such as binding constants and the number of substantive binding sites have been estimated from the analysis of fluorescence quenching measurements. The differences in affinities of curcumin and trans-resveratrol for BLA were compared. The short Förster's distance (r) between donor (BLA) and acceptor (curcumin and trans-resveratrol) and also the binding constant values demonstrated the strong interaction between these two polyphenolic compounds and BLA. The thermodynamic parameters were obtained from the fluorescence quenching measurements in different temperatures. It can be concluded from the sign and magnitude of ∆H and ∆S that the final ligand-protein complexes were stabilized by hydrogen bonds. The considerable change in microregion of the Trp residues in BLA is observed upon the binding of the trans-resveratrol to BLA by synchronous fluorescence while this conforma...Continue Reading

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Citations

Oct 13, 2017·Journal of Medicinal Food·Nydia E Buitimea-CantúaSergio O Serna-Saldívar
Mar 7, 2020·Journal of Biomolecular Structure & Dynamics·Richa MishraSoumendra Rana
Mar 31, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Zhending GanXiang Zhong
Jan 16, 2021·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Hua-Jin ZengLing-Bo Qu
May 19, 2021·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·Mengxue DiaoTiehua Zhang

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