期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 380, 期 2, 页码 377-381出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.103
关键词
Synuclein; Peptide; Metal; Copper; Neurotoxicity
资金
- Alzheimer's Research Trust of the UK [ART/PPG2005B/8]
- Alzheimers Research UK [ART-PPG2005B-8] Funding Source: researchfish
Recent studies have Suggested that alpha-synuclein (AS) is a metal binding protein. Metals also induce protein aggregation. In order to clarify controversy over the location of the metal binding sites six peptide fragments spanning the full length of the protein were analysed to identify metal binding domains. Our results indicated that both the C-terminus of the protein and a region around histidine 50 play a role ill copper binding. We suggest that the true binding domain is a nonlinear site composed of both areas acting together to bind copper. The toxicity of these peptides to SH-SY5Y cells was also Studied. There was a copper-independent component associated with the NAC domain of the protein and a copper-dependent component associated with the C-terminus of the protein and potentiated by involvement of the N-terminus. We hypothesise that copper binding call cause conversion of AS to a neurotoxic form via inter-protein interactions. (C) 2009 Elsevier Inc. All rights reserved
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据