Cited by 1,086Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchPrion Diseases and Protein Misfolding

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A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.

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Hensley, K, Carney, J M, Mattson, M P, Aksenova, M, Harris, M, Wu, J F, Floyd, R A, Butterfield, D A·1994·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.91.8.3270PMC PMC43558

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Abstract

beta-Amyloid is a 39- to 43-amino-acid neurotoxic peptide that aggregates to form the core of Alzheimer disease-associated senile (amyloid) plaques. No satisfactory hypothesis has yet been proposed to explain the mechanism of beta-amyloid aggregation and toxicity. We present mass spectrometric and electron paramagnetic resonance spin trapping evidence that beta-amyloid, in aqueous solution, fragments and generates free radical peptides. beta-Amyloid fragments, at concentrations that previously have been shown to be neurotoxic to cultured neurons, can inactivate oxidation-sensitive glutamine synthetase and creatine kinase enzymes. Also, salicylate hydroxylation assays indicate that reactive oxygen species are generated by the beta-amyloid-(25-35) fragment during cell-free incubation. These results are formulated into a free radical-based unifying hypothesis for neurotoxicity of beta-amyloid and are discussed with reference to membrane molecular alterations in Alzheimer disease.

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Authors: Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A.
Affiliations: University of Kentucky (US)
Department of Chemistry, University of Kentucky, Lexington 40506.
ORCID: Mattson, M P
Aksenova, M
Butterfield, D A
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1994-04-12
Volume: 91
Issue: 8
Pages: 3270-3274
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.91.8.3270
PMC: PMC43558
OpenAlex: W2070117026
Cited by: 1,086
References: 23
Citations by year: 2026: 6 · 2025: 12 · 2024: 20 · 2023: 16 · 2022: 21 · 2021: 26 · 2020: 15 · 2019: 18 · 2018: 26 · 2017: 15 · 2016: 23 · 2015: 27 · 2014: 26 · 2013: 32 · 2012: 34
FWCI: 35.21
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Science Foundation (9108764)
Glenn Foundation for Medical Research
Fondation pour la Recherche Médicale
National Institutes of Health (AG-10836)
National Institute on Aging (AG 09690, P01AG010836, R01AG009690, AG 10836)
Office of Naval Research
National Institute of Neurological Disorders and Stroke (R01NS023307, NS-23307)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: amyloid-beta, amyloid fibril formation, neurotoxicity, free radicals, reactive oxygen species, glutamine synthetase, creatine kinase, salicylate hydroxylation, amyloid plaques, Alzheimer's disease, peptide fragmentation, membrane alterations
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Chromatography, High Pressure Liquid, Electron Spin Resonance Spectroscopy, Free Radicals, Gas Chromatography-Mass Spectrometry, Molecular Sequence Data, Neurotoxins, Salicylates, Amyloid beta-Peptides

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A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.

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