title: [Research on the interaction of aristolochic acid and bovine serum albumin].
abstract: The interaction between aristolochic acid and bovine serum albumin (BSA) under physiological conditions was investigated by fluorescence quenching methods. The results indicate that there is a strong interaction between aristolochic acid and BSA, and the distances between the binding location and tryptophan residue is 2.8 nm. The binding location of aristolochic acid in BSA is in subdomain III A. In addition, the effects of aristolochic acid on the protein second structure were studied using CD and FTIR techniques. The results of CD proved that the alpha-helix contents of BSA decreased from 43.5% to 36.7% after binding with aristolochic acid.
authors.affiliation: Department of Chemistry, Mianyang Teachers College, China.
authors.forename: Jia-qin
authors.initials: JQ
authors.lastname: Liu
authors.forename: Jian-niao
authors.initials: JN
authors.lastname: Tian
authors.forename: Qing-quan
authors.initials: QQ
authors.lastname: Bian
authors.forename: Zhi-de
authors.initials: ZD
authors.lastname: Hu
mesh_terms: D000818:Animals; D034341:Aristolochic Acids / Q000737:chemistry*; D001665:Binding Sites; D002417:Cattle; D010936:Plant Extracts / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D034341:Aristolochic Acids; D010936:Plant Extracts; D012710:Serum Albumin, Bovine