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Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.

Nat Commun. 2015; 
Misra P,, Kodali R,, Chemuru S,, Kar K,, Wetzel R,.
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Biochemicals K4G2Aβ31–42 and K10G2Aβ31–42 (calculated and observed MWs of 1,768.27/1,768.35 and 2,537.31 and 2,537.40, respectively) were obtained from GenScript, Inc. Get A Quote

摘要

Since early oligomeric intermediates in amyloid assembly are often transient and difficult to distinguish, characterize and quantify, the mechanistic basis of the initiation of spontaneous amyloid growth is often opaque. We describe here an approach to the analysis of the Aβ aggregation mechanism that uses Aβ-polyglutamine hybrid peptides designed to retard amyloid maturation and an adjusted thioflavin intensity scale that reveals structural features of aggregation intermediates. The results support an aggregation initiation mechanism for Aβ-polyQ hybrids, and by extension for full-length Aβ peptides, in which a modular Aβ C-terminal segment mediates rapid, non-nucleated formation of α-helical oligomers. ... More

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