The interactions of loureirin A (LA) and Cochinchinenin C (CC) with human serum albumin (HSA) under simulated physiological conditions (pH = 7.4) have been studied with fluorescence, UV-vis absorption spectroscopic method and molecular docking technique. The results indicated that there was a synergistic interaction between LA and Cochinchinenin C, and the fluorescence quenching of HSA by LA (or Cochinchinenin C) was a combined quenching procedure (dynamic and static quenching). At low compound concentrations, the quenching constants KSV of Cochinchinenin C was larger than that of LA, which meant the Cochinchinenin C efficacy may be better than that of LA. The negative ?3H and ?3S values suggested hydrogen bonds and van der Waals forces played the major role in the binding of LA (or Cochinchinenin C) to HSA.