中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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

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