NDLI: Structural conversion of neurotoxic amyloid-β(1

Content Provider	PubMed Central
Author	Ahmed, Mahiuddin Davis, Judianne Aucoin, Darryl Sato, Takeshi Ahuja, Shivani Aimoto, Saburo Elliott, James I. Nostrand, William E. Van Smith, Steven O.
Abstract	The Aβ42 peptide rapidly aggregates to form oligomers, protofibils and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's disease. We show that low temperature and low salt can stabilize disc-shaped oligomers (pentamers) that are significantly more toxic to murine cortical neurons than protofibrils and fibrils. We find that these neurotoxic oligomers do not have the β-sheet structure characteristic of fibrils. Rather, the oligomers are composed of loosely aggregated strands whose C-terminus is protected from solvent exchange and which have a turn conformation placing Phe19 in contact with Leu34. On the basis of NMR spectroscopy, we show that the structural conversion of Aβ42 oligomers to fibrils involves the association of these loosely aggregated strands into β-sheets whose individual β-strands polymerize in a parallel, in-register orientation and are staggered at an inter-monomer contact between Gln15 and Gly37.
Related Links	http://dx.doi.org/10.1038/nsmb.1799
Ending Page	567
Page Count	7
Starting Page	561
File Format	PDF
ISSN	15459993
e-ISSN	15459985
Journal	Nature structural & molecular biology
Issue Number	5
Volume Number	17
Language	English
Publisher Date	2010-05-01
Access Restriction	Open
Subject Keyword	Molecular Biology Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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