Description:
<jats:p>β‐Amyloid deposits, hallmarks of Alzheimer's disease, contain both sugar‐derived ‘advanced glycation end products’ (AGEs) and copper and iron ions. Our <jats:italic>in vitro</jats:italic> experiments using synthetic β‐amyloid peptide and glucose or fructose show that formation of covalently cross‐linked high‐molecular‐mass β‐amyloid peptide oligomers is accelerated by micromolar amounts of copper (Cu<jats:sup>+</jats:sup>, Cu<jats:sup>2+</jats:sup>) and iron (Fe<jats:sup>2+</jats:sup>, Fe<jats:sup>3+</jats:sup>) ions. Formation of these covalent AGE cross‐links can be inhibited by capping agents of amino groups, redox‐inactive metal chelators and antioxidants, suggesting that these drugs may be able to slow down the formation of insoluble β‐amyloid deposits <jats:italic>in vivo</jats:italic> and possibly the progression of Alzheimer's disease.</jats:p>