Molecular spectroscopic studies on the interaction between ractopamine and bovine serum albumin.

To investigate the interaction between Ractopamine (RAC), an animal growth promoter, and bovine serum albumin (BSA), three spectroscopic approaches (fluorescence, UV-vis and FT-IR) and three different experiments (two mole-ratio and a Job's methods) were used to monitor the biological kinetic interaction procedure. The Stern-Volmer quenching constants K(SV), the binding constants K(a), and the number of binding sites n at 298, 301 and 304 K were evaluated by molecular spectroscopic approaches. The values of enthalpy (-13.47 kJ mol(-1)) and entropy (78.39 J mol(-1)K(-1)) in the reaction indicated that RAC bound to BSA mainly by electrostatic and hydrophobic interaction. The site markers competitive experiments indicated that the binding of RAC to BSA primarily took place in site I. The spectra data matrix was further investigated with multivariate curve resolution-alternating least squares (MCR-ALS), and the concentration profiles and the pure spectra for three species (BSA, RAC and RAC-BSA) existed in the kinetic interaction procedure, as well as the apparent equilibrium constants, were obtained.