Cited by 1,046Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchPrion Diseases and Protein Misfolding

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Amyloid β-Protein Fibrillogenesis

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Walsh, Dominic M., Hartley, Dean M., Kusumoto, Yoko, Fezoui, Youcef, Condron, Margaret M., Lomakin, Aleksey, Benedek, George B., Selkoe, Dennis J., Teplow, David B.·1999·Journal of Biological Chemistry

DOI 10.1074/jbc.274.36.25945

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Abstract

Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloid beta-protein (Abeta). Fibrils, both in vitro and in vivo, are neurotoxic. For this reason, substantial effort has been expended to develop therapeutic approaches to control Abeta production and amyloidogenesis. Achievement of the latter goal is facilitated by a rigorous mechanistic understanding of the fibrillogenesis process. Recently, we discovered a novel intermediate in the pathway of Abeta fibril formation, the amyloid protofibril (Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) J. Biol. Chem. 272, 22364-22372). We report here results of studies of the assembly, structure, and biological activity of these polymers. We find that protofibrils: 1) are in equilibrium with low molecular weight Abeta (monomeric or dimeric); 2) have a secondary structure characteristic of amyloid fibrils; 3) appear as beaded chains in rotary shadowed preparations examined electron microscopically; 4) give rise to mature amyloid-like fibrils; and 5) affect the normal metabolism of cultured neurons. The implications of these results for the development of therapies for Alzheimer's disease and for our understanding of fibril assembly are discussed.

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Authors: Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B.
Affiliations: Brigham and Women's Hospital (US)
Massachusetts Institute of Technology (US)
Corresponding author: Teplow, David B.
ORCID: Walsh, Dominic M.
Hartley, Dean M.
Selkoe, Dennis J.
Teplow, David B.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-09
Volume: 274
Issue: 36
Pages: 25945-25952
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.36.25945
OpenAlex: W2073516240
Cited by: 1,046
References: 65
Citations by year: 2026: 5 · 2025: 10 · 2024: 14 · 2023: 15 · 2022: 18 · 2021: 20 · 2020: 24 · 2019: 13 · 2018: 23 · 2017: 26 · 2016: 39 · 2015: 43 · 2014: 38 · 2013: 34 · 2012: 58
FWCI: 21.57
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, 7707 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: Amgen
Brigham and Women's Hospital
Foundation for Neurologic Diseases
National Institutes of Health (5p01ag014366-05)
National Institute on Aging (1PO1 AG14366, 1RO1 AG12749, R01AG012749)
National Institute of Neurological Disorders and Stroke (R01NS038328, 1RO1 NS38328)
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, fibril formation, amyloid protofibrils, Alzheimer's disease, amyloid deposition, neurotoxicity, secondary structure, neuronal metabolism, amyloid fibril formation, Alzheimer's disease treatment
MeSH terms: Alzheimer Disease, Humans, Amyloid beta-Peptides, Protein Structure, Secondary, Protein Folding, Dimerization

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