Interactions of 1-hydroxypyrene with bovine serum albumin: insights from   multi-spectroscopy, docking and molecular dynamics simulation methods

doi:10.1039/c6ra00981f

CORC > 北京大学 > 城市与环境学院

	Interactions of 1-hydroxypyrene with bovine serum albumin: insights from multi-spectroscopy, docking and molecular dynamics simulation methods
	Zhang, Jing ; Chen, Weixiao ; Tang, Bowen ; Zhang, Wei ; Chen, Linfeng ; Duan, Ying ; Zhu, Yuxiu ; Zhu, Yaxian ; Zhang, Yong
刊名	RSC ADVANCES
	2016
关键词	POLYCYCLIC AROMATIC-HYDROCARBONS BINDING-SITE SUBDOMAIN IB PROTEIN FLUORESCENCE SPECTRA PYRENE ACID DRUG RIBOFLAVIN
DOI	10.1039/c6ra00981f
英文摘要	The interaction between a typical PAH metabolite, 1-hydroxypyrene (1-OHP), and a transport protein, bovine serum albumin (BSA), has been investigated using fluorescence, UV-visible absorption (UV-vis), circular dichroism (CD) spectra, docking and molecular dynamics (MD) simulation methods under simulated physiological conditions (in Tris-HCl buffer, pH = 7.40). The experimental results suggested that the fluorescence quenching of BSA by 1-OHP occurred through a mixed static and dynamic quenching mechanism with a binding constant of 2.40 x 10(6) L mol(-1) at 291 K. The thermodynamic parameters together with the docking and MD study revealed that van der Waals forces dominate the formation of the 1-OHP-BSA complex. Applying Forster's non-radiation energy transfer theory, the binding distance of 1-OHP to BSA was calculated to be 2.88 nm. In addition, as confirmed by time resolved fluorescence, UV-vis, three-dimensional (3-D) fluorescence and CD spectra, high concentrations of 1-OHP induced conformational transitions of BSA, increasing the content of the alpha-helix of BSA and exposing its tryptophan residue to a more hydrophilic microenvironment. An inhibition test showed that 1-OHP strongly inhibits the binding constant of vitamin B-2 with BSA. A molecular docking study visualized the binding mode of 1-OHP with BSA. 1-OHP inserted into the binding pocket IB of BSA, leaving its hydroxyl group outside. Based on that, the MD study further unveiled the stability of 1-OHP-BSA complex and their dynamic binding modes, and clarified the contributions of each binding force component and the key residues to the binding process.; National Natural Science Foundation of China [21075102, 21177102, 21577110]; Xiamen University Innovative Research Foundation [DC2013035]; SCI(E); EI; ARTICLE; yzhang@xmu.edu.cn; 28; 23622-23633; 6
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/437980]
专题	城市与环境学院
推荐引用方式 GB/T 7714	Zhang, Jing,Chen, Weixiao,Tang, Bowen,et al. Interactions of 1-hydroxypyrene with bovine serum albumin: insights from multi-spectroscopy, docking and molecular dynamics simulation methods[J]. RSC ADVANCES,2016.
APA	Zhang, Jing.,Chen, Weixiao.,Tang, Bowen.,Zhang, Wei.,Chen, Linfeng.,...&Zhang, Yong.(2016).Interactions of 1-hydroxypyrene with bovine serum albumin: insights from multi-spectroscopy, docking and molecular dynamics simulation methods.RSC ADVANCES.
MLA	Zhang, Jing,et al."Interactions of 1-hydroxypyrene with bovine serum albumin: insights from multi-spectroscopy, docking and molecular dynamics simulation methods".RSC ADVANCES (2016).