A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants

A - Papers appearing in refereed journals

Mohammed-Beigi, H., Kjaer, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., Ward, J. L. and Otzen, D.E. 2019. A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. Frontiers in Plant Science. 10, p. 148.

AuthorsMohammed-Beigi, H., Kjaer, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., Ward, J. L. and Otzen, D.E.
Abstract

The ability of proteins to aggregate to form well-organized β-sheet rich amyloid fibrils is increasingly viewed as a general if regrettable property of the polypeptide chain. Aggregation leads to diseases such as amyloidosis and neurodegeneration in humans and various mammalian species but is also found in a functional variety in both animals and microbes. However, there are to our knowledge no reports of amyloid formation in plants. Plants are also the source of a large number of aggregation-inhibiting compounds. We reasoned that the two phenomena could be connected and that one of (many) preconditions for plant longevity is the ability to suppress unwanted protein aggregation. In support of this, we show that while protein extracts from the sugar maple tree Acer saccharum fibrillate readily on their own, this process is efficiently abolished by addition of small molecule extracts from the same plant. Further analysis of 44 plants showed a correlation between plant longevity and ability to inhibit protein aggregation. Extracts from the best performing plant, the sugar maple, were subjected to chromatographic fractionation, leading to the identification of a large number of compounds, many of which were shown to inhibit aggregation in vitro. One cautious interpretation is that it may have been advantageous for plants to maintain an efficient collection of aggregation-inhibiting metabolites as long as they do not impair metabolite function. From a practical perspective, our results indicate that long-lived plants may be particularly appropriate sources of new anti-aggregation compounds with therapeutic potential.

KeywordsPlant extracts; Plant longevity; Protein aggregation; Inhibitors of aggregation; Aggregate toxicity; Beta amyloid; α-synuclein
Year of Publication2019
JournalFrontiers in Plant Science
Journal citation10, p. 148
Digital Object Identifier (DOI)doi:10.3389/fpls.2019.00148
Open accessPublished as ‘gold’ (paid) open access
FunderBiotechnology and Biological Sciences Research Council
Funder project or codeTPM - Tailoring Plant Metabolism - Work package 2 (WP2) - Designer Willows: high value phenolic glycosides for health and industry
Publisher's version
Output statusPublished
Publication dates
Online13 Feb 2019
Publication process dates
Accepted28 Jan 2019
Copyright licenseCC BY
PublisherFrontiers Media SA
ISSN1664-462X

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