Effect of Aristolochic Acid on the Second Structure of Human Serum Albumin

The binding mode between aristolochic acid and human serum albumin was studied by molecular docking technique. The results indicate that aristolochic acid binds within the subdomain IIA of HSA, and hydrophobic force plays a main role. In addition, the effect of aristolochic acid on the second structure of human serum albumin was investigated using CD and FTIR techniques. As the results of CD proved, the α-helix contents of HSA decreased from 46.6% to 43.6% after binding with aristolochic acid.