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• W2912400124 abstract "Amyloid formation occurs via numerous complex mechanisms, often involving intermediates. This study examines the mechanism of amyloidogenesis in two N-terminal fragments of serum amyloid A (SAA), which are known to exhibit dramatically different amyloid structures. Fibrillization kinetics by these peptides are found to exhibit two unusual features: slower rates at higher peptide concentration, and complete insensitivity to addition of pre-formed seed. Additionally, we find that these peptides form micelle-like oligomers in solution. Our results imply an unusual dual role of micellar oligomers in amyloidogenesis, in which these particles act both as an off-pathway reservoir of peptide, and an inhibitory aggregate that slows amyloid growth. We anticipate that this mechanism of fibril formation may exist in other hydrophobic amyloid-forming peptides and proteins." @default.
• W2912400124 created "2019-02-21" @default.
• W2912400124 creator A5060229634 @default.
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• W2912400124 date "2019-02-27" @default.
• W2912400124 modified "2023-09-27" @default.
• W2912400124 title "Importance of micelle‐like multimers in the atypical aggregation kinetics of N‐terminal serum amyloid A peptides" @default.
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• W2912400124 doi "https://doi.org/10.1002/1873-3468.13334" @default.
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