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Interaction of Curcumin with β-Lactoglobulin—Stability, Spectroscopic Analysis, and Molecular Modeling of the Complex
- Source :
- Journal of Agricultural and Food Chemistry. 58:11130-11139
- Publication Year :
- 2010
- Publisher :
- American Chemical Society (ACS), 2010.
-
Abstract
- Curcumin (diferuloyl methane) is the physiologically and pharmacologically active component of turmeric (Curcuma longa L.). Solubility and stability of curcumin are the limiting factors for realizing its therapeutic potential. β-Lactoglobulin (βLG), the major whey protein, can solubilize and bind many small hydrophobic molecules. The stability of curcumin bound to βLG in solution is enhanced 6.7 times, in comparison to curcumin alone (in aqueous solution). The complex formation of curcumin with βLG has been investigated employing spectroscopic techniques. βLG interacts with curcumin at pH 7.0 with an association constant of 1.04 ± 0.1 × 10(5) M(-1) to form a 1:1 complex at 25 °C. Entropy and free energy changes for the interaction derived from the van't Hoff plot are 18.7 cal mol(-1) K(-1) and -6.8 kcal mol(-1) at 25 °C, respectively; the interaction is hydrophobic in nature. The interaction of βLG with curcumin does not affect either the conformation or the state of association of βLG. Competitive ligand binding measurements, binding studies with denatured βLG, effect of pH on the curcumin-βLG interaction, Forster energy transfer measurements, and molecular docking studies suggest that curcumin binds to the central calyx of βLG. These binding studies have prompted the preparation and encapsulation of curcumin in βLG nanoparticles. Nanoparticles of βLG prepared by desolvation are found to encapsulate curcumin with >96% efficiency. The solubility of curcumin in βLG nanoparticle is significantly enhanced to ∼625 μM in comparison with its aqueous solubility (30 nM). Nanoparticles of βLG, by virtue of their ability to enhance solubility and stability of curcumin, may fit the choice as a carrier molecule.
- Subjects :
- Whey protein
Curcumin
Molecular model
Stereochemistry
Lactoglobulins
Food chemistry
chemistry.chemical_compound
Curcuma
Drug Delivery Systems
Solubility
Beta-lactoglobulin
Drug Carriers
Aqueous solution
biology
Plant Extracts
Protein Stability
Spectrum Analysis
General Chemistry
Hydrogen-Ion Concentration
Combinatorial chemistry
Binding constant
Molecular Docking Simulation
chemistry
biology.protein
General Agricultural and Biological Sciences
Protein Binding
Subjects
Details
- ISSN :
- 15205118 and 00218561
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- Journal of Agricultural and Food Chemistry
- Accession number :
- edsair.doi.dedup.....5716a641a6ce5c1e349bff6fb7eb5f0b