Cited by 522Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchParkinson's Disease Mechanisms and Treatments

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Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins

Chromy, Brett A., Nowak, Richard J., Lambert, Mary P., Viola, Kirsten L., Chang, Lei, Velasco, Pauline T., Jones, Bryan W., Fernandez, Sara J., Lacor, Pascale N., Horowitz, Peleg, Finch, Caleb E., Krafft, Grant A., Klein, William L.·2003·Biochemistry

DOI 10.1021/bi030029q

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Abstract

Amyloid beta 1-42 (Abeta(1-42)) is a self-associating peptide that becomes neurotoxic upon aggregation. Toxicity originally was attributed to the presence of large, readily formed Abeta fibrils, but a variety of other toxic species are now known. The current study shows that Abeta(1-42) can self-assemble into small, stable globular assemblies free of fibrils and protofibrils. Absence of large molecules was verified by atomic force microscopy (AFM) and nondenaturing gel electrophoresis. Denaturing electrophoresis revealed that the globular assemblies comprised oligomers ranging from trimers to 24mers. Oligomers prepared at 4 degrees C stayed fibril-free for days and remained so when shifted to 37 degrees C, although the spectrum of sizes shifted toward larger oligomers at the higher temperature. The soluble, globular Abeta(1-42) oligomers were toxic to PC12 cells, impairing reduction of MTT and interfering with ERK and Rac signal transduction. Occasionally, oligomers were neither toxic nor recognized by toxicity-neutralizing antibodies, suggesting that oligomers could assume alternative conformations. Tests for oligomerization-blocking activity were carried out by dot-blot immunoassays and showed that neuroprotective extracts of Ginkgo biloba could inhibit oligomer formation at very low doses. The observed neurotoxicity, structure, and stability of synthetic Abeta(1-42) globular assemblies support the hypothesis that Abeta(1-42) oligomers play a role in triggering nerve cell dysfunction and death in Alzheimer's disease.

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Abbreviations Aβ, amyloid beta peptide

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Authors: Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., Finch, C. E., Krafft, G. A., & Klein, W. L.
Affiliations: Northwestern University (US)
Corresponding author: Klein, William L.
ORCID: Nowak, Richard J.
Viola, Kirsten L.
Chang, Lei
Horowitz, Peleg
Finch, Caleb E.
Klein, William L.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2003-10-17
Volume: 42
Issue: 44
Pages: 12749-12760
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi030029q
OpenAlex: W1964741226
Cited by: 522
References: 28
Citations by year: 2026: 10 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 11 · 2020: 12 · 2019: 8 · 2018: 17 · 2017: 19 · 2016: 10 · 2015: 26 · 2014: 26 · 2013: 33 · 2012: 37
FWCI: 15.33
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (1p01ag015501-01)
National Institute on Aging (P01-AG15501, R01-AG18877, R01AG018877)
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
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords: amyloid-beta 42, peptide self-assembly, oligomerization, Alzheimer's disease, ERK signaling, Rac signaling, oligomer conformation
MeSH terms: Animals, Epitopes, Body Temperature, Cell Survival, Diffusion, Humans, Ligands, Neurotoxins, Nitroblue Tetrazolium, Peptide Fragments, Plant Extracts, Protein Conformation, Amyloid beta-Peptides, PC12 Cells, Neuroprotective Agents, Ginkgo biloba, Rats

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