title: Transition metal-mediated glycoxidation accelerates cross-linking of beta-amyloid peptide.
abstract: beta-Amyloid deposits, hallmarks of Alzheimer's disease, contain both sugar-derived 'advanced glycation end products' (AGEs) and copper and iron ions. Our in vitro experiments using synthetic beta-amyloid peptide and glucose or fructose show that formation of covalently cross-linked high-molecular-mass beta-amyloid peptide oligomers is accelerated by micromolar amounts of copper (Cu+, Cu2+) and iron (Fe2+, Fe3+) 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 beta-amyloid deposits in vivo and possibly the progression of Alzheimer's disease.
authors.affiliation: Physiological Chemistry I, Biocenter, University of Würzburg, Germany.
authors.forename: C
authors.initials: C
authors.lastname: Loske
authors.forename: A
authors.initials: A
authors.lastname: Gerdemann
authors.forename: W
authors.initials: W
authors.lastname: Schepl
authors.forename: M
authors.initials: M
authors.lastname: Wycislo
authors.forename: R
authors.initials: R
authors.lastname: Schinzel
authors.forename: D
authors.initials: D
authors.lastname: Palm
authors.forename: P
authors.initials: P
authors.lastname: Riederer
authors.forename: G
authors.initials: G
authors.lastname: Münch
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000975:Antioxidants / Q000494:pharmacology; D017127:Glycation End Products, Advanced / Q000502:physiology*; D006031:Glycosylation; D006801:Humans; D008670:Metals / Q000494:pharmacology*; D010710:Phosphates / Q000494:pharmacology
chemical_list: D016229:Amyloid beta-Peptides; D000975:Antioxidants; D017127:Glycation End Products, Advanced; D008670:Metals; D010710:Phosphates