Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
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Abstract
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…
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984
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- 8.59
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- 100%
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Authors
3Topics & keywords
Topics
Keywords
- Chemistry
- Amyloid (mycology)
- Polyphenol
- Small molecule
- Fibril
- Mechanism (biology)
- In vitro
- Biochemistry
UN Sustainable Development Goals
- Good health and well-being
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