Cargando…

Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

Amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity. Consequently, compounds counteracting amyloid aggregation have been investigated for their...

Descripción completa

Detalles Bibliográficos
Autores principales: Stefani, Massimo, Rigacci, Stefania
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3709793/
https://www.ncbi.nlm.nih.gov/pubmed/23765219
http://dx.doi.org/10.3390/ijms140612411
_version_ 1782276804794384384
author Stefani, Massimo
Rigacci, Stefania
author_facet Stefani, Massimo
Rigacci, Stefania
author_sort Stefani, Massimo
collection PubMed
description Amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity. Consequently, compounds counteracting amyloid aggregation have been investigated for their ability (i) to stabilize toxic amyloid precursors; (ii) to prevent the growth of toxic oligomers or speed that of fibrils; (iii) to inhibit fibril growth and deposition; (iv) to disassemble preformed fibrils; and (v) to favor amyloid clearance. Natural phenols, a wide panel of plant molecules, are one of the most actively investigated categories of potential amyloid inhibitors. They are considered responsible for the beneficial effects of several traditional diets being present in green tea, extra virgin olive oil, red wine, spices, berries and aromatic herbs. Accordingly, it has been proposed that some natural phenols could be exploited to prevent and to treat amyloid diseases, and recent studies have provided significant information on their ability to inhibit peptide/protein aggregation in various ways and to stimulate cell defenses, leading to identify shared or specific mechanisms. In the first part of this review, we will overview the significance and mechanisms of amyloid aggregation and aggregate toxicity; then, we will summarize the recent achievements on protection against amyloid diseases by many natural phenols.
format Online
Article
Text
id pubmed-3709793
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Molecular Diversity Preservation International (MDPI)
record_format MEDLINE/PubMed
spelling pubmed-37097932013-07-12 Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds Stefani, Massimo Rigacci, Stefania Int J Mol Sci Review Amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity. Consequently, compounds counteracting amyloid aggregation have been investigated for their ability (i) to stabilize toxic amyloid precursors; (ii) to prevent the growth of toxic oligomers or speed that of fibrils; (iii) to inhibit fibril growth and deposition; (iv) to disassemble preformed fibrils; and (v) to favor amyloid clearance. Natural phenols, a wide panel of plant molecules, are one of the most actively investigated categories of potential amyloid inhibitors. They are considered responsible for the beneficial effects of several traditional diets being present in green tea, extra virgin olive oil, red wine, spices, berries and aromatic herbs. Accordingly, it has been proposed that some natural phenols could be exploited to prevent and to treat amyloid diseases, and recent studies have provided significant information on their ability to inhibit peptide/protein aggregation in various ways and to stimulate cell defenses, leading to identify shared or specific mechanisms. In the first part of this review, we will overview the significance and mechanisms of amyloid aggregation and aggregate toxicity; then, we will summarize the recent achievements on protection against amyloid diseases by many natural phenols. Molecular Diversity Preservation International (MDPI) 2013-06-13 /pmc/articles/PMC3709793/ /pubmed/23765219 http://dx.doi.org/10.3390/ijms140612411 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Stefani, Massimo
Rigacci, Stefania
Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title_full Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title_fullStr Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title_full_unstemmed Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title_short Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds
title_sort protein folding and aggregation into amyloid: the interference by natural phenolic compounds
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3709793/
https://www.ncbi.nlm.nih.gov/pubmed/23765219
http://dx.doi.org/10.3390/ijms140612411
work_keys_str_mv AT stefanimassimo proteinfoldingandaggregationintoamyloidtheinterferencebynaturalphenoliccompounds
AT rigaccistefania proteinfoldingandaggregationintoamyloidtheinterferencebynaturalphenoliccompounds