The Interaction between Tricyclazole and Bovine Serum Albumin by UV and Circular Dichroism
DING Cheng-rong1, GAO Xiao-ru1, XU Li2, ZHANG Guo-fu1, ZHOU Ying1(1.College of Chemical Engineering and Materials Science, Zhejiang University of Technology, Hangzhou 310032, China; 2.Department of Chemistry, Zhejiang University, Hangzhou 310027, China)
The interaction between tricyclazole and bovine serum albumin (BSA) and the effect of different tricyclazole concentration to bovine serum albumin (BSA) had been studied by ultraviolet (UV) and circular dichroism (CD) spectroscopy. The results showed that the effect of tricyclazole to bovine serum albumin was multifaceted. The absorption spectra of UV showed that tricyclazole and bovine serum albumin (BSA) form the ground-state supramolecular complex with intermolecular forces. At the same time, hydrophobic interactions lead to a gradual increase intensity of UV absorption. The CD spectra showed that the peptide chain of BSA occurs contraction and rearrangement because of hydrophobic interactions and intramolecular hydrogen bonds. The conformation of BSA had been changed.