title: Study of the interaction between fisetin and human serum albumin: a biophysical approach.
abstract: The binding of fisetin with human serum albumin (HSA) has been studied at different pH using UV-Vis, FTIR, CD and fluorescence spectroscopic techniques. The binding constants were found to increase with the rise in pH of the media. The negative ΔH°  (kJ mol-1) and positive ΔS°  (J mol-1 K-1) indicate that fisetin binds to HSA via electrostatic interactions with an initial hydrophobic association that result in a positive ΔS° . In presence of potassium chloride (KCl) the binding constants were found to be decrease. The α-helical content of HSA increased after binding with fisetin as analyzed from both CD and FTIR methods. The site marker displacement studies using fluorescence anisotropy suggest that fisetin binds to the hydrophobic pocket (Site 1, subdomain IIA) of HSA which is in good accordance with the molecular docking study. The change in accessible surface area (ASA) of residues of HSA was calculated to get a better insight into the binding.
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Kharagpur-721302, India.
authors.forename: Atanu Singha
authors.initials: AS
authors.lastname: Roy
authors.forename: Amit Kumar
authors.initials: AK
authors.lastname: Dinda
authors.forename: Swagata
authors.initials: S
authors.lastname: Dasgupta
mesh_terms: D055592:Biophysical Phenomena; D005419:Flavonoids / Q000737:chemistry* / Q000378:metabolism; D044948:Flavonols; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D005419:Flavonoids; D044948:Flavonols; D012709:Serum Albumin; C017875:fisetin