The mutual interaction of asiatic acid(AA) with bovine serum albumin(BSA) was investigated using fluorescence spectroscopy. The results revealed that asiatic acid(AA) caused the fluorescence quenching of bovine serum albumin(BSA) through a static quenching procedure. The Stern-Volmer quenching constant were calculated at different temperature. The binding site, apparent binding constant and corresponding thermodynamic parameters ïGo, ïHo, ïSo were calculated and theHydrogen bond andVan derWaals force play an important role in stabilizing the complex. Besides, the effect of Zn2+, Cu2+, Ni2+, Mn2+and Co2+ on the binding constants between asiatic acid(AA) and bovine serumalbumin(BSA) were studied.