IR@PKUHSC  > 北京大学深圳医院
学科主题临床医学
Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach
Wang, Zhen1; Chen, Junhui2; Wang, Shaobin3; Chen, Zhanguang1
关键词Oridonin Bovine Serum Albumin Multispectroscopic Techniques Noncovalent Binding
刊名JOURNAL OF LUMINESCENCE
2013-02-01
DOI10.1016/j.jlumin.2012.06.035
134页:863-869
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Optics
研究领域[WOS]Optics
关键词[WOS]RESONANCE LIGHT-SCATTERING ; NUCLEIC-ACIDS ; ANTICANCER DRUG ; IN-VITRO ; SENSITIVE ASSAY ; BINDING ; DNA ; FLUORESCENCE ; DERIVATIVES ; SYSTEM
英文摘要

Oridonin is an effective anticancer drug which has high potency and low systemic toxicity. In this study, the interaction between oridonin and bovine serum albumin (BSA) was investigated by several spectroscopic approaches for the first time. The binding characteristics of oridonin and BSA were determined by fluorescence emission spectra and resonance light scattering spectra. It is showed that the oridonin quenches the fluorescence of BSA and the static quenching constant K-SV is 1.30 x 10(4) L mol(-1) at 298 K. Moreover, oridonin and BSA form a 1:1 complex with a binding constant of 0.62 x 104 L mol(-1). On the other hand, the thermodynamic parameters indicate that the binding process was a spontaneous molecular interaction procedure, in which hydrophobic forces played a major role. The structure analysis indicates that oridonin binding results in an increased hydrophobicity around the tryptophan residues of BSA. Additionally, as shown by the UV-vis absorption, synchronous fluorescence and three-dimensional fluorescence results, oridonin could lead to conformational and some microenvironmental changes of BSA. The work provides accurate and full basic data for clarifying the binding mechanism of oridonin with BSA in vitro and is helpful for understanding its effect on protein function during its transportation and distribution in blood. (c) 2012 Elsevier B.V. All rights reserved.

语种英语
WOS记录号WOS:000313393300136
Citation statistics
Cited Times:13[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/56409
Collection北京大学深圳医院
作者单位1.Shantou Univ, Dept Chem, Shantou 515063, Peoples R China
2.Fourth Peoples Hosp Shenzhen, Shenzhen 518033, Peoples R China
3.Peking Univ, Shenzhen Hosp, Intervent Oncol & Minimally Invas Therapies Dept, Shenzhen 518036, Peoples R China
Recommended Citation
GB/T 7714
Wang, Zhen,Chen, Junhui,Wang, Shaobin,et al. Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach[J]. JOURNAL OF LUMINESCENCE,2013,134:863-869.
APA Wang, Zhen,Chen, Junhui,Wang, Shaobin,&Chen, Zhanguang.(2013).Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach.JOURNAL OF LUMINESCENCE,134,863-869.
MLA Wang, Zhen,et al."Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach".JOURNAL OF LUMINESCENCE 134(2013):863-869.
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