The interaction between amlodipine and bovine serum albumin(BSA) was investigated by a combined spectral and computational approach.The result showed that BSA fluorescence at 342 nm is quenched regularly with the addition of amlodipine,which belongs to the static fluorescence quenching and the binding mechanism is related to the fluorescence resonance energy transfer(FRET).According to Lineweaver-Burk equation,the binding constants between amlodipine and BSA are 1.214×104 L?mol-1(296 K) and 1.662×104 L?mol-1(303 K),respectively.The calculated thermodynamic parameters(ΔH=33.46 kJ?mol-1,ΔS=19122 J?mol-1?K-1) by Van’t Hoff equation showed that hydrophobic interaction plays a major role in the amlodipine-BSA system.The binding of amlodipine and BSA is a spontaneous inter-molecular interaction driven by entropy.Molecular modeling displayed that amlodipine is bound in the large hydrophobic cavity of BSA,which accords well with the result from the spectral experiment.