Stereoselective interaction of cinchona alkaloid isomers with bovine serum albumin.

摘要: The dependence of the interaction between bovine serum albumin (BSA) and two cinchona alkaloids, quinine (QN) quinidine (QD), on absolute configuration these stereoisomers has been comprehensively studied. FTIR spectra showed that QN QD interacted with both CO C–N groups BSA, resulting in changes to secondary structure protein. Fluorescence quenching BSA by revealed lower efficiency for Trp emission when compared QN. Further analysis accurately described different binding behaviors recognition discrepancies towards which was reflected through affinities, driving forces, energy conformational during ligand–protein interactions. Synchronous fluorescence further proved farther from Tyr than This work could provide basic data clarifying interaction, metabolism distribution alkaloid vivo.