Probing the binding sites and the effect of berbamine on the structure of bovine serum albumin.

摘要: Abstract Berbamine, a naturally occurring isoquinoline alkaloid extracted from Berberis sp., is the active constituent of some Chinese herbal medicines and exhibits variety pharmacological activities. The effects berbamine on structure bovine serum albumin (BSA) were investigated by circular dichroism, fluorescence absorption spectroscopy under physiological conditions. Berbamine caused static quenching intrinsic BSA, data analyzed application Stern–Volmer equation. There was single primary berbamine-binding site BSA with binding constant 2.577 × 10 4  L mol −1 at 298 K. thermodynamic parameters, enthalpy change (Δ H 0 ) entropy S for reaction −76.5 kJ mol −173.4 J mol  K according to van’t Hoff results showed that hydrogen bond van der Waals interaction predominant forces in process. Competitive experiments revealed displacement warfarin berbamine, indicating located Drug sites I. distance r between donor acceptor (berbamine) obtained Forster non-radiation energy transfer theory. three-dimensional spectra, UV–vis difference spectra dichroism presence conformation changed. provide quantitative understanding effect albumin, providing useful guideline further drug design.