title: Investigation of the binding of Salvianolic acid B to human serum albumin and the effect of metal ions on the binding.
abstract: The studies on the interaction between HSA and drugs have been an interesting research field in life science, chemistry and clinical medicine. There are also many metal ions present in blood plasma, thus the research about the effect of metal ions on the interaction between drugs and plasma proteins is crucial. In this study, the interaction of Salvianolic acid B (Sal B) with human serum albumin (HSA) was investigated by the steady-state, synchronous fluorescence and circular dichroism (CD) spectroscopies. The results showed that Sal B had a strong ability to quench the intrinsic fluorescence of HSA through a static quenching mechanism. Binding parameters calculated showed that Sal B was bound to HSA with the binding affinities of 10(5) L mol(-1). The thermodynamic parameters studies revealed that the binding was characterized by positive enthalpy and positive entropy changes, and hydrophobic interactions were the predominant intermolecular forces to stabilize the complex. The specific binding distance r (2.93 nm) between donor (HSA) and acceptor (Sal B) was obtained according to Förster non-radiative resonance energy transfer theory. The synchronous fluorescence experiment revealed that Sal B cannot lead to the microenvironmental changes around the Tyr and Trp residues of HSA, and the binding site of Sal B on HSA is located in hydrophobic cavity of subdomain IIA. The CD spectroscopy indicated the secondary structure of HSA is not changed in the presence of Sal B. Furthermore, The effect of metal ions (e.g. Zn(2+), Cu(2+), Co(2+), Ni(2+), Fe(3+)) on the binding constant of Sal B-HSA complex was also discussed.
authors.affiliation: School of Chemistry and Chemical Engineering, Nantong University, Nantong 226019, PR China.
authors.forename: Tingting
authors.initials: T
authors.lastname: Chen
authors.forename: Hui
authors.initials: H
authors.lastname: Cao
authors.forename: Shajun
authors.initials: S
authors.lastname: Zhu
authors.forename: Yapeng
authors.initials: Y
authors.lastname: Lu
authors.forename: Yanfang
authors.initials: Y
authors.lastname: Shang
authors.forename: Miao
authors.initials: M
authors.lastname: Wang
authors.forename: Yanfeng
authors.initials: Y
authors.lastname: Tang
authors.forename: Li
authors.initials: L
authors.lastname: Zhu
mesh_terms: D001572:Benzofurans / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites / Q000187:drug effects; D002942:Circular Dichroism; D004347:Drug Interactions; D006801:Humans; D007477:Ions / Q000494:pharmacology; D008670:Metals / Q000494:pharmacology*; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D053630:Depsides
chemical_list: D001572:Benzofurans; D007477:Ions; D008670:Metals; D012709:Serum Albumin; C076944:salvianolic acid B; D053630:Depsides