Journal
ACS CHEMICAL NEUROSCIENCE
Volume 11, Issue 19, Pages 2915-2934Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschemneuro.0c00381
Keywords
Protein aggregates; polyphenols; alpha-synuclein; amyloid-beta; Alzheimer's disease; Parkinson's disease
Funding
- NIH [1SC3 GM111200 01A1, R25GM069621-17]
- Les and Harriet Dodson Endowment
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One of the main features of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease is the amyloidogenic behavior of disease-specific proteins including amyloid beta, tau, alpha-synuclein, and mutant Huntingtin which participate in the formation, accumulation, and deposition of toxic misfolded aggregates. Consequently, these proteins not only associated with the progress of their respective neurodegenerative pathologies but also qualify as disease-specific biomarkers. The aim of using natural polyphenols is to target amyloid-dependent proteopathies by decreasing free radical damage and inhibiting and dissolving amyloid fibrils. We explore the effectiveness of the polyphenols epigallocatechin-3-gallate, oleuropein aglycone, and quercetin on their ability to inhibit aggregation of amyloid beta, tau, and a-synuclein and mitigate other pathological features for Alzheimer's disease and Parkinson's disease. The analysis was carried from in vitro and cell line studies to animal models and clinical trials. This Review describes the use of phytochemical compounds as prophylactic agents for Alzheimer's disease, Parkinson's disease, and other proteopathies.
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