Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation
文献类型：期刊论文
| 作者 | Li, HT; Du, HN; Tang, L; Hu, J; Hu, HY |
| 刊名 | BIOPOLYMERS
 |
| 出版日期 | 2002 |
| 卷号 | 64期号:4页码:221-226 |
| 关键词 | alpha-synuclein trifluoroethanol non-amyloid component segment beta-sheet aggregation |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China., |
| 英文摘要 | Amyloid-like aggregation of alpha-synuclein and deposit in Lewy bodies arc thought to be the major cause of Parkinson's disease. Here we describe the secondary structural transformation and aggregation of human alpha-synuclein and its C-terminus truncated fragments in trifluoroethanol. Proteins containing the NAC (non-amyloid component) segment undergo a three-state transition: from native random coil to beta-sheet and to alpha-helical structure, while the NAC deficient fragment and gamma-synuclein undergo a typical two-state coil-to-alpha transition. The beta-sheet form is highly hydrophobic that strongly binds to 1-anilinonaphthalene-8-sulfonic acid (ANS) and is prone to self-aggregation. The results suggest that the NAC sequence is essential to beta-sheet formation and the aggregation originates from the beta-sheet intermediate, which may be implicated in the pathogenesis of Parkinson's disease. (C) 2002 Wiley Periodicals, Inc. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | PARKINSONS-DISEASE ; CONFORMATION ; ALZHEIMERS ; PROTEINS ; STATE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000176388900005 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2475]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Li, HT,Du, HN,Tang, L,et al. Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation[J]. BIOPOLYMERS,2002,64(4):221-226. |
| APA | Li, HT,Du, HN,Tang, L,Hu, J,&Hu, HY.(2002).Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation.BIOPOLYMERS,64(4),221-226. |
| MLA | Li, HT,et al."Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: Non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation".BIOPOLYMERS 64.4(2002):221-226. |
入库方式： OAI收割
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。