Aluminium, beta-amyloid and non-enzymatic glycosylation

FEBS Lett. 1995 May 8;364(2):182-4. doi: 10.1016/0014-5793(95)00388-p.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aluminum / toxicity*
  • Alzheimer Disease / etiology
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / drug effects*
  • Amyloid beta-Peptides / ultrastructure
  • Cross-Linking Reagents
  • Glycosylation
  • Humans
  • In Vitro Techniques
  • Macromolecular Substances
  • Microscopy, Electron
  • Protein Conformation / drug effects

Substances

  • Amyloid beta-Peptides
  • Cross-Linking Reagents
  • Macromolecular Substances
  • Aluminum