Spearmint Extract Containing Rosmarinic Acid Suppresses Amyloid Fibril Formation of Proteins Associated with Dementia

Neurological dementias such as Alzheimer's disease and Lewy body dementia are thought to be caused in part by the formation and deposition of characteristic insoluble fibrils of polypeptides such as amyloid beta (Aβ), Tau, and/or α-synuclein (αSyn). In this context, it is critical to suppress a...

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Bibliographic Details
Published in:	Nutrients Vol. 12; no. 11; p. 3480
Main Authors:	Ogawa, Kenjirou, Ishii, Ayumi, Shindo, Aimi, Hongo, Kunihiro, Mizobata, Tomohiro, Sogon, Tetsuya, Kawata, Yasushi
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 13-11-2020 MDPI
Subjects:	alpha-Synuclein Alzheimer Disease Alzheimer's disease Amyloid - pharmacology amyloid beta Amyloid beta-Peptides amyloid fibril Benzothiazoles Biocompatibility Cell Line Cell Survival - drug effects Cinnamates - pharmacology Dementia Dementia disorders Depsides - pharmacology E coli Fibrillogenesis Humans Lewy bodies Mentha spicata - chemistry Parkinson's disease Peptides Plant Extracts - pharmacology Polypeptides polyphenol Polyphenols Proteins Rosmarinic Acid spearmint Synuclein Tau protein Transmission electron microscopy United States > US Japan Tau dementia rosmarinic acid amyloid fibril alpha-synuclein polyphenol spearmint amyloid beta
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Summary:	Neurological dementias such as Alzheimer's disease and Lewy body dementia are thought to be caused in part by the formation and deposition of characteristic insoluble fibrils of polypeptides such as amyloid beta (Aβ), Tau, and/or α-synuclein (αSyn). In this context, it is critical to suppress and remove such aggregates in order to prevent and/or delay the progression of dementia in these ailments. In this report, we investigated the effects of spearmint extract (SME) and rosmarinic acid (RA; the major component of SME) on the amyloid fibril formation reactions of αSyn, Aβ, and Tau proteins in vitro. SME or RA was added to soluble samples of each protein and the formation of fibrils was monitored by thioflavin T (ThioT) binding assays and transmission electron microscopy (TEM). We also evaluated whether preformed amyloid fibrils could be dissolved by the addition of RA. Our results reveal for the first time that SME and RA both suppress amyloid fibril formation, and that RA could disassemble preformed fibrils of αSyn, Aβ, and Tau into non-toxic species. Our results suggest that SME and RA may potentially suppress amyloid fibrils implicated in the progression of Alzheimer's disease and Lewy body dementia in vivo, as well.
ISSN:	2072-6643 2072-6643
DOI:	10.3390/nu12113480