Alzheimer’s disease is a progressive neurodegenerative disease that is characterized by the presence of extracellular amyloid plaques and intraneuronal neurofibrillary tangles within the brain. Biochemical analysis of amyloid plaques have revealed that the main constituents are fibrillary aggregates of 39-42 peptide residues referred to as the amyloid-β protein (Aβ). Here, we examined the consecutive aggregation stages of the Aβ-42 peptide, as well as the fibril formation stages on a mica substrate by using atomic force microscopy. These results offer new tools for an analysis of the mechanisms of Aβ aggregation.
Alzheimer’s disease is a progressive neurodegenerative disease that is characterized by the presence of extracellular amyloid plaques and intraneuronal neurofibrillary tangles within the brain. Biochemical analysis of amyloid plaques have revealed that the main constituents are fibrillary aggregates of 39-42 peptide residues referred to as the amyloid-β protein (Aβ). Here, we examined the consecutive aggregation stages of the Aβ-42 peptide, as well as the fibril formation stages on a mica substrate by using atomic force microscopy. These results offer new tools for an analysis of the mechanisms of Aβ aggregation.
