globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1721220115
论文题名:
Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils
作者: Ruggeri F.S.; Benedetti F.; Knowles T.P.J.; Lashuel H.A.; Sekatskii S.; Dietler G.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:28
起始页码: 7230
结束页码: 7235
语种: 英语
英文关键词: Amyloid ; Atomic force microscopy ; Early molecular assembly ; Force spectroscopy ; Protein aggregation
Scopus关键词: alpha synuclein ; alpha synuclein ; amyloid ; SNCA protein, human ; Article ; atomic force microscopy ; biophysics ; controlled study ; molecular mechanics ; nonhuman ; oligomerization ; priority journal ; protein analysis ; protein assembly ; protein function ; protein unfolding ; chemistry ; human ; metabolism ; Parkinson disease ; pathology ; protein unfolding ; proteinosis ; ultrastructure ; alpha-Synuclein ; Amyloid ; Humans ; Microscopy, Atomic Force ; Parkinson Disease ; Protein Aggregation, Pathological ; Protein Unfolding
英文摘要: The formation and spreading of amyloid aggregates from the presynaptic protein α-synuclein in the brain play central roles in the pathogenesis of Parkinson’s disease. Here, we use high-resolution atomic force microscopy to investigate the early oligomerization events of α-synuclein with single monomer angstrom resolution. We identify, visualize, and characterize directly the smallest elementary unit in the hierarchical assembly of amyloid fibrils, termed here single-strand protofilaments. We show that protofilaments form from the direct molecular assembly of unfolded monomeric α-synuclein polypeptide chains. To unravel protofilaments’ internal structure and elastic properties, we manipulated nano-mechanically these species by atomic force spectroscopy. The single-molecule scale identification and characterization of the fundamental unit of amyloid assemblies provide insights into early events underlying their formation and shed light on opportunities for therapeutic intervention at the early stages of aberrant protein self-assembly. © 2018 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163694
Appears in Collections:气候变化与战略

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作者单位: Ruggeri, F.S., Laboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, 1015, Switzerland, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom; Benedetti, F., Centre for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Lausanne, 1015, Switzerland; Knowles, T.P.J., Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom, Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge, CB3 0HE, United Kingdom; Lashuel, H.A., Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Faculty of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, 1015, Switzerland; Sekatskii, S., Laboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, 1015, Switzerland; Dietler, G., Laboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, 1015, Switzerland

Recommended Citation:
Ruggeri F.S.,Benedetti F.,Knowles T.P.J.,et al. Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(28)
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