Resveratrol, genistein, and curcumin bind bovine serum albumin.

摘要: We report the complexation of bovine serum albumin (BSA) with resveratrol, genistein, and curcumin, at physiological conditions, using constant protein concentration various polyphenol contents. FTIR, CD, fluorescence spectroscopic methods were used to analyze ligand binding mode, constant, effects on BSA stability conformation. Structural analysis showed that polyphenols bind via hydrophilic hydrophobic interactions number bound (n) being 1.30 for resveratrol−BSA, genisten−BSA, 1.0 curcumin−BSA. The polyphenol−BSA constants KRes−BSA = 2.52(±0.5) × 104 M−1, KGen−BSA 1.26(±0.3) KCur−BSA 3.33(±0.8) M−1. Polyphenol altered conformation a major reduction α-helix an increase in β-sheet turn structures, indicating partial unfolding.