Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM
文献类型：期刊论文
| 作者 | Zhang, F ; Lin, XJ ; Ji, LN ; Du, HN ; Tang, L(唐琳） ; He, JH（何建华） ; Hu, J（胡钧） ; Hu, HY |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2008 |
| 卷号 | 368期号:2页码:388 |
| ISSN号 | 0006-291X |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China |
| 英文摘要 | alpha-Synuclein (alpha-Syn) fibrils are the major component of Lewy bodies that are closely associated with the pathogenesis of Parkinson's disease, but the mechanism for the fibril assembly remains poorly understood. Here we report using a combination of peptide truncation and atomic force microscopy (AFM) to elucidate the self-assembly and morphology of the alpha-Syn fibrils. The results show that protease K significantly slims the fibrils from the mean height of similar to 6.6 to similar to 4.7 nm, whereas chaotropic denaturant urea completely breaks down the fibrils into small particles. The in situ enzymatic digestion also results in thinning of the fibrils, giving rise to some nicks on the fibrils. Moreover, N- or C-terminally truncated alpha-Syn fragments assemble into thinner filaments with the heights depending on the peptide lengths. A nine-residue peptide corresponding to the homologous GAV-motif sequence can form very thin (similar to 2.2 nm) but long (> 1 mu m) filaments. Thus, the central sequence of alpha-Syn forms a fibrillar core by cross-beta-structure that is flanked by two flexible termini, and the orientation of the fibril growth is perpendicular to the P-sheet structures. (c) 2008 Elsevier Inc. All rights reserved. |
| 学科主题 | Physics |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000253669500035 |
| 公开日期 | 2012-04-18 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/7656]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2004-2010年 |
| 推荐引用方式 GB/T 7714 | Zhang, F,Lin, XJ,Ji, LN,et al. Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2008,368(2):388. |
| APA | Zhang, F.,Lin, XJ.,Ji, LN.,Du, HN.,Tang, L.,...&Hu, HY.(2008).Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,368(2),388. |
| MLA | Zhang, F,et al."Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 368.2(2008):388. |
入库方式： OAI收割
来源：上海应用物理研究所
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。