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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 PublicationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN0006-291X
Volume368Issue:2Pages:388
Abstractalpha-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 AreaPhysics
Indexed BySCI
Language英语
Funding Project应物所项目组
WOS IDWOS:000253669500035
Citation statistics
Cited Times:10[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/7656
Collection中科院上海应用物理研究所2004-2010年
Corresponding AuthorHu, 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.
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