Knowledge Management System Of Shanghai Institute of Applied Physics, CAS
| Assembly of alpha-synuclein fibrils in nanoscale studied by peptide truncation and AFM | |
| Zhang, F; Lin, XJ; Ji, LN; Du, HN; Tang, L(唐琳）; He, JH（何建华）; Hu, J（胡钧）; Hu, HY; 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 | |
| 2008 | |
| Source Publication | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| ISSN | 0006-291X |
| Volume | 368Issue:2Pages:388 |
| Abstract | 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. |
| Subject Area | Physics |
| Indexed By | SCI |
| Language | 英语 |
| Funding Project | 应物所项目组 |
| WOS ID | WOS:000253669500035 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.sinap.ac.cn/handle/331007/7656 |
| Collection | 中科院上海应用物理研究所2004-2010年 |
| Corresponding Author | 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 |
| Recommended Citation 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. |
| Files in This Item: | ||||||
| File Name/Size | DocType | Version | Access | License | ||
| Assembly of alpha-sy（1318KB） | 开放获取 | -- | View Application Full Text | |||
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Edit Comment