Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods.

ABSTRACT: Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 104 L/mol (298 K), 6.17 × 104 L/mol (305 K) and 5.73 × 104 L/mol (312 K) at pH 2.0, which was greater than that (3.98 × 104 L/mol at 298 K, 3.90 × 104 L/mol at 305 K and 3.41 × 104 L/mol at 312 K) at pH 7.4. Molecular docking study showed that binding energy of β-casein-curcumin complex at pH 2.0 (-7.53 kcal/mol)

SUBMITTER: Zhao R 

PROVIDER: S-EPMC8398086 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature