title: 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.
abstract: Isoimperatorin is one of the main components of Prangos ferulacea as a linear furanocoumarin and used as anti-inflammatory, analgesic, antispasmodic, and anticancer drug. Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. Since the carrying of drug by HSA may affect on its structure and action, we decided to investigate the interaction between HSA and isoimperatorin using fluorescence and UV spectroscopy. Fluorescence data indicated that isoimperatorin quenches the intrinsic fluorescence of the HSA via a static mechanism and hydrophobic interaction play the major role in the drug binding. The binding average distance between isoimperatorin and Trp 214 of HSA was estimated on the basis of the theory of Förster energy transfer. Decrease of protein surface hydrophobicity (PSH) was also documented upon isoimperatorin binding. Furthermore, the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues does not have obvious changes. Site marker compettive and fluorescence experiments revealed that the binding of isoimperatorin to HSA occurred at or near site I. Finally, the binding details between isoimperatorin and HSA were further confirmed by molecular docking and esterase activity inhibition studies which revealed that drug was bound at subdomain IIA.
authors: Nano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, Iran.
authors: Samira
authors: S
authors: Ranjbar
authors: Yalda
authors: Y
authors: Shokoohinia
authors: Sirous
authors: S
authors: Ghobadi
authors: Nooshin
authors: N
authors: Bijari
authors: Saeed
authors: S
authors: Gholamzadeh
authors: Nastaran
authors: N
authors: Moradi
authors: Mohammad Reza
authors: MR
authors: Ashrafi-Kooshk
authors: Abbas
authors: A
authors: Aghaei
authors: Reza
authors: R
authors: Khodarahmi
mesh_terms: D001665:Binding Sites; D004950:Esterases / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
chemical_list: D012709:Serum Albumin; D014364:Tryptophan; D004950:Esterases