Aluminium, β-amyloid and non-enzymatic glycosylation

AbstractThe non-enzymatic glycosylation of β-amyloid is implicated in the aetiology of Alzheimer's disease. However, controversy surrounds the nature of any involvement and a potential mechanism has not been fully elucidated. We present evidence of an aluminium-induced aggregation of the AβP(25–35) peptide and speculate that the mechanism of formation of our ordered β-amyloid aggregates might involve non-enzymatic glycosylation and/or site-specific crosslinking of β-amyloid fibrils by atomic aluminium