Importance of micelle-like multimers in the atypical aggregation kinetics of N-terminal serum amyloid A peptides.

摘要: Amyloid formation occurs via numerous complex mechanisms, often involving intermediates. This study examines the mechanism of amyloidogenesis in two N-terminal fragments serum amyloid A (SAA), which are known to exhibit dramatically different structures. Fibrillization kinetics by these peptides found unusual features: slower rates at higher peptide concentration, and complete insensitivity addition pre-formed seed. Additionally, we find that form micelle-like oligomers solution. Our results imply an dual role micellar amyloidogenesis, particles act both as off-pathway reservoir peptide, inhibitory aggregate slows growth. We anticipate this fibril may exist other hydrophobic amyloid-forming proteins.