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Acceleration of Amyloid Fibril Formation by Specific Binding of Aβ-(1–40) Peptide to Ganglioside-containing Membrane Vesicles
Open accessAbstract
The interaction of Alzheimer's Abeta peptide and its fluorescent analogue with membrane vesicles was studied by spectrofluorometry, Congo Red binding, and electron microscopy. The peptide binds selectively to the membranes containing gangliosides with a binding affinity ranging from 10(-6) to 10(-7) M depending on the type of ganglioside sugar moiety. This interaction appears to be ganglioside-specific as under our experimental conditions (neutral pH, physiologically relevant ionic strength), no Abeta binding was observed to ganglioside-free membranes containing zwitterionic or acidic phospholipids. Importantly, the addition of ganglioside-containing vesicles to the peptide solution dramatically accelerates the rate of fibril formation as compared with that of the peptide alone. The present results strongly suggest that the membrane-bound form of the peptide may act as a specific "template" (seed) that catalyzes the fibrillogenesis process in vivo.
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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
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Hydrogen peroxide mediates amyloid β protein toxicity
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RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
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Cholesterol, lipid rafts, and disease
Simons, K., & Ehehalt, R. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216390 · Cited by 916
Cholesterol-Dependent γ-Secretase Activity in Buoyant Cholesterol-Rich Membrane Microdomains
Wahrle, S., Das, P., Nyborg, A. C., McLendon, C., Shoji, M., Kawarabayashi, T., Younkin, L. H., Younkin, S. G., & Golde, T. E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0470 · Cited by 356
Gangliosides in the Brain: Physiology, Pathophysiology and Therapeutic Applications
Sipione, S., Monyror, J., Galleguillos, D., Steinberg, N., & Kadam, V. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.572965 · Cited by 325
Kawarabayashi, T., Shoji, M., Younkin, L. H., Wen-Lang, L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., & Younkin, S. G. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5543-03.2004 · Cited by 320
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290
Metadata
- Authors
- Choo-Smith, L.-P., Garzon-Rodriguez, W., Glabe, C. G., & Surewicz, W. K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-09
- Volume
- 272
- Issue
- 37
- Pages
- 22987-22990
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2130079515
- Cited by
- 312
- References
- 6
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Acceleration of Amyloid Fibril Formation by Specific Binding of Aβ-(1–40) Peptide to Ganglioside-containing Membrane Vesicles. https://app.cochat.ai/papers/10.1074/jbc.272.37.22987
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- Choo-Smith, L.-P., Garzon-Rodriguez, W., Glabe, C. G., & Surewicz, W. K. (1997). Acceleration of Amyloid Fibril Formation by Specific Binding of Aβ-(1–40) Peptide to Ganglioside-containing Membrane Vesicles. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.37.22987
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
