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Aluminium, β‐amyloid and non‐enzymatic glycosylation
Author(s) -
Christopher Exley,
Laurent Schley,
S. B. Murray,
Carole M. Hackney,
J. D. Birchall
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00388-p
Subject(s) - glycosylation , chemistry , amyloid (mycology) , enzyme , peptide , biochemistry , senile plaques , biochemistry of alzheimer's disease , mechanism (biology) , amyloid beta , amyloid precursor protein , biophysics , alzheimer's disease , biology , disease , medicine , inorganic chemistry , philosophy , epistemology
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.