Aarhus University Seal

Daniel Otzen

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

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. / Mohammad-Beigi, Hossein; Kjær, Lars; Eskandari, Hoda et al.

In: Frontiers in Plant Science, Vol. 10, No. 148, 148, 2019.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Mohammad-Beigi, H, Kjær, L, Eskandari, H, Aliakbari, F, Christiansen, G, Ruvo, G, L. Ward, J & Otzen, D 2019, 'A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants', Frontiers in Plant Science, vol. 10, no. 148, 148. https://doi.org/10.3389/fpls.2019.00148

APA

Mohammad-Beigi, H., Kjær, L., Eskandari, H., Aliakbari, F., Christiansen, G., Ruvo, G., L. Ward, J., & Otzen, D. (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(148), [148]. https://doi.org/10.3389/fpls.2019.00148

CBE

MLA

Vancouver

Mohammad-Beigi H, Kjær L, Eskandari H, Aliakbari F, Christiansen G, Ruvo G et al. A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants. Frontiers in Plant Science. 2019;10(148):148. doi: 10.3389/fpls.2019.00148

Author

Bibtex

@article{ada474f8779c45b897820b36774b44df,
title = "A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants",
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.",
keywords = "Aggregate toxicity, Beta amyloid, Inhibitors of aggregation, Plant extracts, Plant longevity, Protein aggregation, α-synuclein, CORE, MECHANISM, inhibitors of aggregation, plant extracts, TOXICITY, ALPHA-SYNUCLEIN, alpha-synuclein, PEPTIDE, aggregate toxicity, beta amyloid, protein aggregation, plant longevity",
author = "Hossein Mohammad-Beigi and Lars Kj{\ae}r and Hoda Eskandari and Farhang Aliakbari and Gunna Christiansen and Gianluca Ruvo and {L. Ward}, Jane and Daniel Otzen",
year = "2019",
doi = "10.3389/fpls.2019.00148",
language = "English",
volume = "10",
journal = "Frontiers in Plant Science",
issn = "1664-462X",
publisher = "Frontiers Media S.A",
number = "148",

}

RIS

TY - JOUR

T1 - A Possible Connection Between Plant Longevity and the Absence of Protein Fibrillation: Basis for Identifying Aggregation Inhibitors in Plants

AU - Mohammad-Beigi, Hossein

AU - Kjær, Lars

AU - Eskandari, Hoda

AU - Aliakbari, Farhang

AU - Christiansen, Gunna

AU - Ruvo, Gianluca

AU - L. Ward, Jane

AU - Otzen, Daniel

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

KW - Aggregate toxicity

KW - Beta amyloid

KW - Inhibitors of aggregation

KW - Plant extracts

KW - Plant longevity

KW - Protein aggregation

KW - α-synuclein

KW - CORE

KW - MECHANISM

KW - inhibitors of aggregation

KW - plant extracts

KW - TOXICITY

KW - ALPHA-SYNUCLEIN

KW - alpha-synuclein

KW - PEPTIDE

KW - aggregate toxicity

KW - beta amyloid

KW - protein aggregation

KW - plant longevity

UR - http://www.scopus.com/inward/record.url?scp=85062410429&partnerID=8YFLogxK

U2 - 10.3389/fpls.2019.00148

DO - 10.3389/fpls.2019.00148

M3 - Journal article

C2 - 30815009

VL - 10

JO - Frontiers in Plant Science

JF - Frontiers in Plant Science

SN - 1664-462X

IS - 148

M1 - 148

ER -