The non-enzymatic glycosylation of beta-amyloid is implicated in the a
etiology of Alzheimer's disease, However, controversy surrounds the na
ture of any involvement and a potential mechanism has not been fully e
lucidated, We present evidence of an aluminium-induced aggregation of
the A beta P(25-35) peptide and speculate that the mechanism of format
ion of our ordered beta-amyloid aggregates might involve non-enzymatic
glycosylation and/or site-specific crosslinking of beta-amyloid fibri
ls by atomic aluminium.