Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein

摘要: Isoimperatorin is one of the main components Prangos ferulacea as a linear furanocoumarin and used anti-inflammatory, analgesic, antispasmodic, anticancer drug. Human serum albumin (HSA) principal extracellular protein with high concentration in blood plasma carrier for many drugs to different molecular targets. Since carrying drug by HSA may affect on its structure action, we decided investigate interaction between isoimperatorin using fluorescence UV spectroscopy. Fluorescence data indicated that quenches intrinsic via static mechanism hydrophobic play major role binding. The binding average distance Trp 214 was estimated basis theory Forster energy transfer. Decrease surface hydrophobicity (PSH) also documented upon Furthermore, synchronous spectra show microenvironment tryptophan residues does not have obvious changes. Site marker compettive experiments revealed occurred at or near site I. Finally, details were further confirmed docking esterase activity inhibition studies which bound subdomain IIA.