The 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. © 1995 Federation of European Biochemical Societies. All rights reserved.
Exley, C., Schley, L., Murray, S., Hackney, C. M., & Birchall, J. D. (1995). Aluminium, β-amyloid and non-enzymatic glycosylation. FEBS Letters, 364(2), 182–184. https://doi.org/10.1016/0014-5793(95)00388-P