UM
Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling
Li, Yan; Chen, Chun; Zhang, Chunping; Duan, Jingyu; Yao, Huankai; Wei, Qunli
2017
Source PublicationJOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
ISSN0739-1102
Volume35Issue:6Pages:1189-1199
AbstractHuman 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-alpha-L-arabinofuranosyl-kaempferol-7-O-alpha-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 ERP. These results unravel the binding interaction of AKR with HSA and mechanism as an ERs modulator.
Keywordhuman serum albumin flavonoid binding interaction fluorescence spectroscopy molecular docking
DOI10.1080/07391102.2016.1174622
URLView the original
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000400177700003
PublisherTAYLOR & FRANCIS INC
The Source to ArticleWOS
Fulltext Access
Citation statistics
Cited Times [WOS]:6   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionUniversity of Macau
Recommended Citation
GB/T 7714
Li, Yan,Chen, Chun,Zhang, Chunping,et al. Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling[J]. JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS,2017,35(6):1189-1199.
APA Li, Yan,Chen, Chun,Zhang, Chunping,Duan, Jingyu,Yao, Huankai,&Wei, Qunli.(2017).Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS,35(6),1189-1199.
MLA Li, Yan,et al."Probing the binding interaction of AKR with human serum albumin by multiple fluorescence spectroscopy and molecular modeling".JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS 35.6(2017):1189-1199.
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