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Binding of vanadium compounds perturbs conformation and aggregation state of insulin
Yang, XG1; Yang, XD1; Li, RC1; Wang, K1
关键词Insulin Vanadium Compounds Conformation
刊名PROGRESS IN NATURAL SCIENCE
2003
13期:1页:39-45
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Materials Science, Multidisciplinary ; Multidisciplinary Sciences
研究领域[WOS]Materials Science ; Science & Technology - Other Topics
关键词[WOS]ALLOSTERIC TRANSITION ; RECEPTOR-BINDING ; HEXAMER ; ZINC ; COORDINATION ; ENHANCEMENT ; DERIVATIVES ; CHEMISTRY ; OXIDATION ; PROTEINS
英文摘要

The interactions between zinc-free insulin and vanadium compounds, NaVO3, VO(acac)(2) and VO(ma)(2), have been investigated by fluorescence spectroscopy, circular dichroism (CD) and Fourier-transformed infrared (FT-IR) spectroscopy. The results showed that binding of vanadium compounds produced a static quenching of the intrinsic fluorescence of insulin. The apparent association constants were determined to be (0.17 +/- 0.01) X 10(4) L(.)mol(-1) for NaVO3, (2.8 +/- 0.2) X 10(4) L-mol(-1) for VO(acac)(2), and(4.0 +/- 0.1) X 10(4) L(.)mol(-1) for VO(ma)(2), respectively. The light scattering intensity of insulin decreased upon incubation with the vanadium compounds, suggesting the disaggregation of insulin. The attenuation of the band at 273 nm of insulin CD spectra also supported the disaggregation of insulin observed above. A new band at 1650 similar to 1653 cm(-1) appeared in the FT-IR spectra of insulin upon incubation with the vanadium compounds, indicating the formation of an a-helix structure at B (9-19) motif. This alpha-helix structure suggests a structural change of insulin from an extended conformation (T state) to a helical conformation (R state), which is essential for binding of insulin to its receptor. In conclusion, binding of vanadium compounds results in conformational changes and disaggregation of insulin. These changes might account for the enhancement of binding affinity for insulin to its receptor in the presence of vanadium compounds.

语种英语
WOS记录号WOS:000180469300006
引用统计
被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/50657
专题北京大学药学院_化学生物学系
作者单位1.Peking Univ, Sch Pharmaceut Sci, Dept Biol Chem, Div Bioinorgan Chem, Beijing 100083, Peoples R China
2.Peking Univ, Natl Res Labs Nat Biomimet Drugs, Beijing 100083, Peoples R China
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GB/T 7714
Yang, XG,Yang, XD,Li, RC,et al. Binding of vanadium compounds perturbs conformation and aggregation state of insulin[J]. PROGRESS IN NATURAL SCIENCE,2003,13(1):39-45.
APA Yang, XG,Yang, XD,Li, RC,&Wang, K.(2003).Binding of vanadium compounds perturbs conformation and aggregation state of insulin.PROGRESS IN NATURAL SCIENCE,13(1),39-45.
MLA Yang, XG,et al."Binding of vanadium compounds perturbs conformation and aggregation state of insulin".PROGRESS IN NATURAL SCIENCE 13.1(2003):39-45.
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