Cited by 83Alzheimer's disease research and treatmentsMedicinal Plants and NeuroprotectionParkinson's Disease Mechanisms and Treatments

Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies

Henríquez, Gabriela, Gomez, Alejandra, Guerrero, Erick, Narayan, Mahesh·2020·ACS Chemical Neuroscience

Abstract

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 β, tau, α-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 β, tau, and α-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.

Integrity signals

Registry

Crossref · 10.1021/acschemneuro.0c00381

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246 of 246 references verified0 citation errors · 0 not checkable

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Authors
Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M.
Affiliations
  • Department of Environmental Science and Engineering, the University of Texas at El Paso (UTEP), El Paso, Texas 79968, United States
  • The University of Texas at El Paso (US)
Corresponding author
Narayan, Mahesh
Venue
ACS Chemical Neuroscience
Published
2020-08-21
Volume
11
Issue
19
Pages
2915-2934
ISSN
1948-7193 (ISSN-L)
OpenAlex
W3080099077
Cited by
83
References
246
Citations by year
2026: 8 · 2025: 13 · 2024: 15 · 2023: 21 · 2022: 16 · 2021: 8 · 2020: 2
FWCI
1.53
Type
journal article
Language
en
Open access
closed
Locations
  • ACS Chemical Neuroscience (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Health and Human Services (#R25GM069621-11, 1SC3 GM111200 01A1)
  • Les and Harriet Dodson Endowment
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Complementary and alternative medicine › Medicinal Plants and Neuroprotection
  • Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Keywords
natural polyphenols, protein aggregation, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, amyloid-beta, tau protein, alpha-synuclein, huntingtin, epigallocatechin gallate, oleuropein aglycone, quercetin, proteinopathies, oxidative damage, neuroprotection
MeSH terms
Alzheimer Disease, Animals, Amyloid beta-Peptides, alpha-Synuclein, Polyphenols, Protein Aggregates

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