title: Molecular docking and reaction kinetic studies of chrysin binding to serum albumin.
abstract: The binding properties of chrysin with serum albumin (SA) were investigated under physiological conditions by calorimetry, circular dichroism (CD) spectroscopy, and molecular modeling. Based on the thermodynamic data, molar reaction enthalpy, reaction order (n) and the rate constant (k) were calculated. The results of CD spectroscopy showed that chrysin could bind to SA and the conformation of SA did not have any high-ordered structural change. Computational mapping revealed chrysin binding to the subdomain IB in SA. The chrysin-serum albumin complex was stabilized by hydrophobic force and hydrogen bonding and the reaction was a spontaneous process.
authors.forename: Bingli
authors.initials: B
authors.lastname: Jiang
authors.forename: Anran
authors.initials: A
authors.lastname: Zhao
authors.forename: Jianhua
authors.initials: J
authors.lastname: Miao
authors.forename: Pengfei
authors.initials: P
authors.lastname: Chang
authors.forename: Hailin
authors.initials: H
authors.lastname: Chen
authors.forename: Weigao
authors.initials: W
authors.lastname: Pan
authors.forename: Cuiwu
authors.initials: C
authors.lastname: Lin
mesh_terms: D002942:Circular Dichroism; D005419:Flavonoids / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D062105:Molecular Docking Simulation / Q000379:methods*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*
chemical_list: D005419:Flavonoids; D012709:Serum Albumin; C043561:chrysin