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Study of the interaction of Zn^2+ with Aβ(10-21) by fluorescamine assay
作者姓名:Chao  Feng  Zhang  Li  Fan  Pin  Yang
作者单位:Chao Feng Zhang Li Fan Pin Yang~* Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education,Institute of Molecular Science,Shanxi University,Taiyuan 030006,China
基金项目:This work was supported by the National Natural Science Foundation of China (No. 30470408).
摘    要:Zinc may play a role as a co-factor in the pathogenesis of Alzheimer's disease(AD)through influencing the conformation and neurotoxicity of amyloidβ-protein(Aβ).Using the fluorescamine assay,we show for the first time that Zn~(2 )induced Aβ(10-21) aggregate in a concentration-dependent manner.These results indicate that Aβ(10-21)can be used as an in vitro model in Zn~(2 )- induced Aβaggregation and that the region 10-21 to be the minimal fragment of zinc-binding domain of full length Aβ(1-42).

关 键 词:Aβ(10-21)  Fluorescamine  Zn~(2  )  Aggregation
收稿时间:2006-05-12

Study of the interaction of Zn2+ with Aβ(10-21) by fluorescamine assay
Chao Feng Zhang Li Fan Pin Yang.Study of the interaction of Zn2+ with Aβ(10-21) by fluorescamine assay[J].Chinese Chemical Letters,2007,18(1):97-98.
Authors:Chao Feng Zhang  Li Fan  Pin Yang  
Institution:Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Molecular Science, Shanxi University, Taiyuan 030006, China
Abstract:Zinc may play a role as a co-factor in the pathogenesis of Alzheimer's disease (AD) through influencing the conformation and neurotoxicity of amyloid β-protein (Aβ). Using the fluorescamine assay, we show for the first time that Zn2+ induced Aβ(10-21) aggregate in a concentration-dependent manner. These results indicate that Aβ(10-21) can be used as an in vitro model in Zn2+-induced Aβ aggregation and that the region 10-21 to be the minimal fragment of zinc-binding domain of full length Aβ(1-42).
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