Journal
REDOX-ACTIVE METALS IN NEUROLOGICAL DISORDERS
Volume 1012, Issue -, Pages 164-170Publisher
NEW YORK ACAD SCIENCES
DOI: 10.1196/annals.1306.013
Keywords
Alzheimer's disease; ascorbate; beta-amyloid peptide (beta AP); CU2+; oxidation; sequence
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Funding
- NIA NIH HHS [2P01AG12993] Funding Source: Medline
- NATIONAL INSTITUTE ON AGING [P01AG012993] Funding Source: NIH RePORTER
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This review summarizes tandem mass spectrometric investigations on the selectivity of metal-catalyzed oxidation of beta-amyloid peptide (PAP) and related sequences. A remarkable feature of the Cu2+/ascorbate-dependent oxidation of these peptides is the switch from predominantly His oxidation in the neurotoxic peptide betaAPl-40 to predominantly Tyr oxidation in the nonneurotoxic reverse sequence betaAP40-1. Within betaAPI-40, His(13) and His(14) of the high-affinity Cu2+-binding site are most sensitive to oxidation. Eventually, the oxidation of one or both of these His residues could result in a less redox-active betaAP-Cu2+ complex, lowering the incidence of betaAP-Cu2+-dependent Fenton-type reactions for the benefit of surrounding biological tissue.
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