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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mohammadi, Fakhrossadat Moeeni, Marzieh
Description	Author Affiliation: Mohammadi F ( Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731, Iran. Electronic address: fmohammadi@iasbs.ac.ir.); Moeeni M ( Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731, Iran.)
Abstract	The ability of bovine -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 conformation alteration was not observed upon interaction with curcumin. It was indicated by docking studies that curcumin come closer to the Trp-118 than to other tryptophans and trans-resveratrol binds in the vicinity of Trp-60 and Trp-104. Docking studies indicated that these two compounds bind to BLA by two hydrogen bonds. The calculated distances between bound ligands and tryptophans obtained by docking studies were in agreement with fluorescence resonance energy transfer results. Therefore, the strong interaction of curcumin and trans-resveratrol with BLA was confirmed by theoretical and experimental studies. These achieved results may be applicable in the milk industry and drug formulation.
File Format	HTM / HTML
ISSN	09284931
Volume Number	50
e-ISSN	18730191
Journal	Materials Science and Engineering: C
Language	English
Publisher	Elsevier
Publisher Date	2015-05-01
Publisher Place	Netherlands
Access Restriction	Subscribed
Subject Keyword	Discipline Materials Science Curcumin Chemistry Metabolism Lactalbumin Molecular Docking Simulation Stilbenes Animals Binding Sites Cattle Hydrogen Bonding Kinetics Ligands Molecular Conformation Protein Binding Spectrometry, Fluorescence Thermodynamics Tryptophan Journal Article
Content Type	Text
Resource Type	Article
Subject	Mechanics of Materials Biomaterials Condensed Matter Physics Bioengineering Mechanical Engineering

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