title: Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.
abstract: Human serum albumin (HSA) is the major transport protein affording endogenous and exogenous substances in plasma. It can affect the behavior and efficacy of chemicals in vivo through the binding interaction. AKR (3-O-α-l-arabinofuranosyl-kaempferol-7-O-α-l-rhamnopyranoside) is a flavonoid diglycoside with modulation of estrogen receptors (ERs). Herein, we investigated the binding interaction between AKR and HSA by multiple fluorescence spectroscopy and molecular modeling. As a result, AKR specifically binds in site I of HSA through hydrogen bonds, van der Waals force, and electrostatic interaction. The formation of AKR-HSA complex in binding process is spontaneously exothermic and leads to the static fluorescence quenching through affecting the microenvironment around the fluorophores. The complex also affects the backbone of HSA and makes AKR access to fluorophores. Molecular modeling gives the visualization of the interaction between AKR and HSA as well as ERs. The affinity of AKR with HSA is higher than the competitive site marker Warfarin. In addition, docking studies reveal the binding interaction of AKR with ERs through hydrogen bonds, van der Waals force, hydrophobic, and electrostatic interactions. And AKR is more favorable to ERβ. These results unravel the binding interaction of AKR with HSA and mechanism as an ERs modulator.
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.
authors.forename: Chun
authors.initials: C
authors.lastname: Chen
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.
authors.forename: Chunping
authors.initials: C
authors.lastname: Zhang
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.
authors.forename: Jingyu
authors.initials: J
authors.lastname: Duan
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.|b Faculty of Health Sciences , University of Macau , Macau SAR , Taipa , China.
authors.forename: Huankai
authors.initials: H
authors.lastname: Yao
authors.affiliation: a School of Pharmacy and Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy , Xuzhou Medical University , Xuzhou , Jiangsu 221004 , China.
authors.forename: Qunli
authors.initials: Q
authors.lastname: Wei
mesh_terms: D001665:Binding Sites; D006027:Glycosides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D044949:Kaempferols / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods; D013816:Thermodynamics
chemical_list: D006027:Glycosides; D044949:Kaempferols; D012709:Serum Albumin; C516876:kaempferol-7-O-alpha-L-rhamnopyranoside
keywords: binding interaction; flavonoid; fluorescence spectroscopy; human serum albumin; molecular docking