Affect of Leukamenin E on secondary structure of bovine serum albumin(BSA) is studied by ultraviolet(UV) and circular dichroism(CD) spectroscopy.The results show that the intensity of UV absorption on 230 nm and 278 nm has increased when the mole ratio of Leukamenin E to BSA at 6∶1,15∶1,20∶1.In the same condition,the continuesly increasing concentration of Leukamenin E could lead a gradually increasing intensity of CD absorption,the concentration of α-helix raise from 61.36% to 70.68%.It shows that the interaction between Leukamenin E and BSA increases hydrophobic interactions,leads to the peptide chain of BSA occurs contraction and rearrangement and changes the conformation of BSA.