Anti-amyloidoGenic Effects of Soybean Isoflavones In Vitro: Fluorescence Spectroscopy Demonstrating Direct Binding to Aβ Monomers, Oligomers and Fibrils
Open accessAbstract
Alzheimer's disease is characterized by the presence of extracellular deposits of amyloid, primarily composed of the amyloid β-protein (Aβ). A growing body of evidence indicates that oligomeric forms of Aβ play a critical role in disease causation. Soybean isoflavones are flavonoids with an isoflavone backbone. Isoflavones have been reported to protect against Aβ-induced neurotoxicity in cultured cell systems, the molecular mechanisms remain unclear. Our previous studies demonstrated that red wine-related flavonoids with a flavone backbone are able to inhibit Aβ assembly and destabilize preformed Aβ aggregates. Here, we show that isoflavones, especially glycitein and genistein, have anti-fibrillization, anti-oligomerization and fibril-destabilizing effects on Aβ(1-40) and Aβ(1-42)in vitro at physiological pH and temperature, by using nucleation-dependent polymerization monitored by thioflavin T fluorescence, atomic force microscopy, electron microscopy, and photo-induced cross-linking of unmodified proteins followed by SDS-PAGE. Our three-dimensional fluorescence spectroscopic analyses demonstrated that glycitein interacted with Aβ monomers, oligomers and fibrils, indicating specific binding of glycitein to these Aβ species. Glycitein also interacted with different Aβ fragments (Aβ(1-42), Aβ(1-40), Aβ(1-16) and Aβ(25-35)), exhibiting the highest fluorescence enhancement with Aβ(25-35). We speculated that glycitein's anti-amyloidogenic properties are specifically mediated by its binding to Aβ monomers, oligomers and fibrils. Isoflavones may hold promise as a treatment option for preventative strategies targeting amyloid formation in Alzheimer's disease.
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Genistein directly binds Aβ25-35 fragment preventing formation of its aggregates.
“Hirohata et al. (2012) observed that genistein can directly bind the Aβ25-35 fragment preventing the formation of its aggregates.”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Hirohata et al., 2012
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- Authors
- Hirohata, M., Ono, K., Takasaki, J.-I., Takahashi, R., Ikeda, T., Morinaga, A., & Yamada, M.
- Affiliations
- Kanazawa University (JP)
- Corresponding author
- Yamada, Masahito
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 1822
- Issue
- 8
- Pages
- 1316-1324
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2074581769
- Cited by
- 43
- References
- 34
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 6 · 2021: 3 · 2020: 4 · 2019: 1 · 2018: 3 · 2017: 1 · 2015: 4 · 2014: 4 · 2013: 2 · 2012: 1
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Knowledge Cluster Initiative [High-Tech Sensing and Knowledge Handling Technology (Brain Technology)]
- Grant-in-Aid for Scientific Research (B) (20390242)
- Japanese Ministry of Education, Culture, Sports, Science and Technology, Japan
- Ministry of Health, Labour, and Welfare, Japan (M.Y.)
- Novartis Foundation for Gerontological Research
- Nagao Memorial Foundation
- Alumni Association of the School of Medicine at Showa University
- Fuji Foundation for Protein Research
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pathology and Forensic Medicine › Phytoestrogen effects and research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- soy isoflavones, glycitein, genistein, amyloid-beta, Alzheimer's disease, amyloid oligomers, amyloid fibrils, protein-protein binding, amyloid beta 25-35, flavonoids, thioflavin T
- MeSH terms
- Humans, Isoflavones, Microscopy, Electron, Peptide Fragments, Glycine max, Spectrometry, Fluorescence, Thiazoles, Amyloid beta-Peptides, Microscopy, Atomic Force, Benzothiazoles
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