The interactions between human serum albumin(HSA)and five kinds of amino acid enantiomers were studied by surface plasmon resonance (SPR) without any labeling for the first time.The dynamic informations of their interactions were well shown in real time,and the kinetics parameters were also obtained.The difference in interactions between each of amino acid enantiomers and HSA could be recognized obviously by comparison of the sensorgrams.Although the binding rate constants and the dissociation rate constants of them did not have any rule,the results showed that the affinity of HSA and L-amino acid was bigger than that of HSA and D-amino acid,which indicated the chiral recognition force may contribute to the discrimination interactions between amino acid enantiomers and HSA.