Diplazium esculentum (Retz.) Sw. reduces BACE-1 activities and amyloid peptides accumulation in Drosophila models of Alzheimer's disease.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
10 12 2021
Historique:
received: 01 08 2021
accepted: 26 11 2021
entrez: 11 12 2021
pubmed: 12 12 2021
medline: 27 1 2022
Statut: epublish

Résumé

Alzheimer's disease (AD), one type of dementia, is a complex disease affecting people globally with limited drug treatment. Thus, natural products are currently of interest as promising candidates because of their cost-effectiveness and multi-target abilities. Diplazium esculentum (Retz.) Sw., an edible fern, inhibited acetylcholinesterase in vitro, inferring that it might be a promising candidate for AD treatment by supporting cholinergic neurons. However, evidence demonstrating anti-AD properties of this edible plant via inhibiting of neurotoxic peptides production, amyloid beta (Aβ), both in vitro and in vivo is lacking. Thus, the anti-AD properties of D. esculentum extract both in vitro and in Drosophila models of Aβ-mediated toxicity were elucidated. Findings showed that an ethanolic extract exhibited high phenolics and flavonoids, contributing to antioxidant and inhibitory activities against AD-related enzymes. Notably, the extract acted as a BACE-1 blocker and reduced amyloid beta 42 (Aβ42) peptides in Drosophila models, resulting in improved locomotor behaviors. Information gained from this study suggested that D. esculentum showed potential for AD amelioration and prevention. Further investigations in vertebrates or humans are required to determine the effective doses of D. esculentum against AD, particularly via amyloidogenic pathway.

Identifiants

pubmed: 34893659
doi: 10.1038/s41598-021-03142-w
pii: 10.1038/s41598-021-03142-w
pmc: PMC8664832
doi:

Substances chimiques

Amyloid beta-Peptides 0
Antioxidants 0
Biological Products 0
Biomarkers 0
Peptide Fragments 0
Phytochemicals 0
Plant Extracts 0
Protein Aggregates 0
amyloid beta-protein (1-42) 0
Amyloid Precursor Protein Secretases EC 3.4.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

23796

Informations de copyright

© 2021. The Author(s).

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Auteurs

Thanit Kunkeaw (T)

Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.

Uthaiwan Suttisansanee (U)

Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.

Dunyaporn Trachootham (D)

Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.

Jirarat Karinchai (J)

Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.

Boonrat Chantong (B)

Department of Preclinical Science and Applied Animal Science, Faculty of Veterinary Science, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.

Saranyapin Potikanond (S)

Department of Pharmacology, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.

Woorawee Inthachat (W)

Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.

Pornsiri Pitchakarn (P)

Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.

Piya Temviriyanukul (P)

Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand. piya.tem@mahidol.ac.th.

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Classifications MeSH