The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Open accessAbstract
The formation of well‐ordered fibrillar protein deposits is common to a large group of amyloid‐associated disorders. This group consists of several major human diseases such as Alzheimer's disease, Parkinson's disease, prion diseases, and type II diabetes. Currently, there is no approved therapeutic agent directed towards the formation of fibrillar assemblies, which have been recently shown to have a key role in the cytotoxic nature of amyloidogenic proteins. One important approach in the development of therapeutic agents is the use of small molecules that specifically and efficiently inhibit the aggregation process. Several small polyphenol molecules have been demonstrated to remarkably inhibit the formation of fibrillar assemblies in vitro and their associated cytotoxicity. Yet, the inhibition mechanism was mostly attributed to the antioxidative properties of these polyphenol compounds. Based on several observations demonstrating that polyphenols are capable of inhibiting amyloid fibril formation in vitro, regardless of oxidative conditions, and in view of their structural similarities we suggest an additional mechanism of action. This mechanism is assuming structural constraints and specific aromatic interactions, which direct polyphenol inhibitors to the amyloidogenic core. This proposed mechanism is highly relevant for future de novo inhibitors‘ design as therapeutic agents for the treatment of amyloid‐associated diseases.
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Cites
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Cited by
Plant Polyphenols: Chemical Properties, Biological Activities, and Synthesis
Quideau, S., Deffieux, D., Douat‐Casassus, C., & Pouységu, L. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201000044 · Cited by 2,730
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Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Review on Alzheimer’s Disease: Inhibition of Amyloid Beta and Tau Tangle Formation
Ashrafian, H., Zadeh, E. H., & Khan, R. H. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.192 · Cited by 368
Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan
Alavez, S., Vantipalli, M. C., Zucker, D. J. S., Klang, I. M., & Lithgow, G. J. (2011) · Nature · doi:10.1038/nature09873 · Cited by 361
Metadata
- Authors
- Porat, Y., Abramowitz, A., & Gazit, E.
- Venue
- Chemical Biology & Drug Design
- Publisher
- Wiley
- Published
- 2005-12-16
- Volume
- 67
- Issue
- 1
- Pages
- 27-37
- ISSN
- 1747-0277 (ISSN-L)
- 1747-0285
- OpenAlex
- W2020069228
- Cited by
- 989
- References
- 68
- FWCI
- 9.49
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Porat, Y., Abramowitz, A., & Gazit, E. (2006). Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism. Chemical Biology & Drug Design. https://doi.org/10.1111/j.1747-0285.2005.00318.x
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