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Int. J. Mol. Sci. 2013, 14(6), 12411-12457; doi:10.3390/ijms140612411
Review

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

1,2,*  and 1
Received: 19 April 2013; in revised form: 29 May 2013 / Accepted: 4 June 2013 / Published: 13 June 2013
(This article belongs to the Special Issue Protein Folding 2015)
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Abstract: 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.
Keywords: amyloid; amyloid aggregation; polyphenols; natural phenols amyloid; amyloid aggregation; polyphenols; natural phenols
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Stefani, M.; Rigacci, S. Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds. Int. J. Mol. Sci. 2013, 14, 12411-12457.

AMA Style

Stefani M, Rigacci S. Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds. International Journal of Molecular Sciences. 2013; 14(6):12411-12457.

Chicago/Turabian Style

Stefani, Massimo; Rigacci, Stefania. 2013. "Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds." Int. J. Mol. Sci. 14, no. 6: 12411-12457.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert