title: Aluminium, beta-amyloid and non-enzymatic glycosylation.
abstract: The non-enzymatic glycosylation of beta-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 A beta P(25-35) peptide and speculate that the mechanism of formation of our ordered beta-amyloid aggregates might involve non-enzymatic glycosylation and/or site-specific crosslinking of beta-amyloid fibrils by atomic aluminium.
authors.affiliation: Department of Chemistry, Keele University, Staffordshire, UK.
authors.forename: C
authors.initials: C
authors.lastname: Exley
authors.forename: L
authors.initials: L
authors.lastname: Schley
authors.forename: S
authors.initials: S
authors.lastname: Murray
authors.forename: C M
authors.initials: CM
authors.lastname: Hackney
authors.forename: J D
authors.initials: JD
authors.lastname: Birchall
mesh_terms: D000535:Aluminum / Q000633:toxicity*; D000544:Alzheimer Disease / Q000209:etiology; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000187:drug effects* / Q000648:ultrastructure; D003432:Cross-Linking Reagents; D006031:Glycosylation; D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D011487:Protein Conformation / Q000187:drug effects
chemical_list: D016229:Amyloid beta-Peptides; D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D000535:Aluminum