Cited by 1,015Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis

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Stine, W. Blaine, Dahlgren, Karie N., Krafft, Grant A., LaDu, Mary Jo·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m210207200

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Abstract

Extensive research causally links amyloid-beta peptide (A beta) to Alzheimer's disease, although the pathologically relevant A beta conformation remains unclear. A beta spontaneously aggregates into the fibrils that deposit in senile plaques. However, recent in vivo and in vitro reports describe a potent biological activity for oligomeric assemblies of A beta. To consistently prepare in vitro oligomeric and fibrillar forms of A beta 1-42, a detailed knowledge of how solution parameters influence structure is required. This manuscript represents the first study using a single chemically and structurally homogeneous unaggregated starting material to demonstrate that the formation of oligomers, fibrils, and fibrillar aggregates is determined by time, concentration, temperature, pH, ionic strength, and A beta species. We recently reported that oligomers inhibit neuronal viability 10-fold more than fibrils and approximately 40-fold more than unaggregated peptide, with oligomeric A beta 1-42-induced neurotoxicity significant at 10 nm. In addition, we were able to differentiate by structure and neurotoxic activity wild-type A beta1-42 from isoforms containing familial mutations (Dahlgren, K. N., Manelli, A. M., Stine, W. B., Jr., Baker, L. K., Krafft, G. A., and LaDu, M. J. (2002) J. Biol. Chem. 277, 32046-32053). Understanding the biological role of specific A beta conformations may define the link between A beta and Alzheimer's disease, re-focusing therapeutic approaches by identifying the pernicious species of A beta ultimately responsible for the cognitive dysfunction that defines the disease.

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Authors: Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J.
Affiliations: Northwestern University (US)
Corresponding author: LaDu, Mary Jo
ORCID: LaDu, Mary Jo
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-03
Volume: 278
Issue: 13
Pages: 11612-11622
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m210207200
OpenAlex: W2133631618
Cited by: 1,015
References: 74
Citations by year: 2026: 40 · 2025: 39 · 2024: 37 · 2023: 39 · 2022: 34 · 2021: 49 · 2020: 37 · 2019: 40 · 2018: 33 · 2017: 46 · 2016: 49 · 2015: 42 · 2014: 60 · 2013: 52 · 2012: 69
FWCI: 19.08
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6422 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Alzheimer's Association
Northwestern University
National Institutes of Health (1p01ag015501-01, 5r01ag013496-05)
National Institute on Aging (R01AG019121, AG-15501, AG 19121, AG13496)
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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, amyloid-beta 42, oligomerization, fibril formation, Alzheimer's disease, neurotoxicity, peptide aggregation, solution conditions, familial Alzheimer's disease mutations, amyloid plaques, peptide conformation
MeSH terms: Biopolymers, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Peptide Fragments, Solubility, Blotting, Western, Amyloid beta-Peptides

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In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis

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