Study of the interaction of kaempferol with bovine serum albumin

摘要: Abstract The binding of kaempferol with bovine serum albumin (BSA) was investigated at three temperatures, 296, 310 and 318 K, by the fluorescence, circular dichroism (CD) Fourier transform infrared spectroscopy (FT-IR) pH 7.40. CD FT-IR studies indicate that binds strongly to BSA. association constant K determined Stern–Volmer equation based on quenching fluorescence BSA in presence kaempferol. thermodynamic parameters were calculated according dependence enthalpy change temperature as follows: Δ H 0 S possess small negative (−1.694 kJ/mol) positive values (88.814 J/mol K), respectively. According displacement experimental results, it is considered site II (subdomain III) mainly hydrophobic interaction. results studied experiments secondary structures protein have been changed interaction distance between tryptophan residues bound estimated be 2.78 nm using Foster's basis energy transfer.