Cited by 1,014Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchPrion Diseases and Protein Misfolding

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Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

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Burdick, D, Soreghan, B, Kwon, M, Kosmoski, J, Knauer, M, Henschen, A, Yates, J, Cotman, C, Glabe, C·1992·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)48529-8

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Abstract

The amyloid A4 or beta peptide is a major component of extracellular amyloid deposits that are a characteristic feature of Alzheimer's disease. We synthesized a series of peptide analogs of the A4/beta peptide which are progressively longer at their carboxyl termini, including 42- and 39-residue peptides which represent the major forms of the A4/beta peptide in senile plaque and the hereditary cerebral hemorrhage with amyloidosis form, respectively. All peptides tested, beta 1-28 through beta 1-42, formed amyloid-like fibrils and previously unreported thin sheet-like structures which stained with thioflavin T and Congo Red. The solubility of beta 1-42 and shorter peptides was pH and concentration dependent, with a broad insolubility profile in the pH range of 3.5-6.5 and at concentrations above 0.75 mg/ml. Only peptides of 42 residues or longer were significantly insoluble at pH 7.4. beta 1-47 and beta 1-52 peptides are highly insoluble in aqueous media but are soluble at 40 mg/ml in the alpha helix-promoting solvent, 1,1,1,3,3,3-hexafluoro-2-propanol. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the beta 1-42 peptide migrates as a series of higher molecular mass aggregates whereas shorter peptides migrate as monomers. Aggregation is also dependent on pH, peptide concentration, and time of incubation in aqueous medium. These results indicate that the length of the hydrophobic carboxyl terminus of the A4/beta peptide is important in determining the s…

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Authors: Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C.
Affiliations: University of California, Irvine (US)
ORCID: Henschen, A
Yates, J
Cotman, C
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-01
Volume: 267
Issue: 1
Pages: 546-554
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)48529-8
OpenAlex: W2130144581
Cited by: 1,014
References: 42
Citations by year: 2026: 7 · 2025: 8 · 2024: 14 · 2023: 21 · 2022: 14 · 2021: 29 · 2020: 20 · 2019: 22 · 2018: 28 · 2017: 27 · 2016: 30 · 2015: 29 · 2014: 37 · 2013: 29 · 2012: 31
FWCI: 28.77
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10516 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (1r35ag007918-01, 5r01hd021379-14)
National Institute on Aging (AG07918)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD21379)
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, Alzheimer's disease, peptide analogues, amyloid fibril formation, peptide aggregation, solubility, pH dependence, Congo red staining, thioflavin T staining, amyloid plaques, hexafluoroisopropanol, amyloid deposition
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Amyloid, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Kinetics, Microscopy, Electron, Molecular Sequence Data, Peptides, Mass Spectrometry, Amyloid beta-Peptides

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Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

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