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Secondary Metabolites from Plants Possessing Inhibitory Properties against Beta-Amyloid Aggregation as Revealed by Thioflavin-T Assay and Correlations with Investigations on Transgenic Mouse Models of Alzheimer's Disease.

Authors :
Stefanescu, Raluca
Stanciu, Gabriela Dumitriṭa
Luca, Andrei
Paduraru, Luminita
Tamba, Bogdan-Ionel
Source :
Biomolecules (2218-273X); Jun2020, Vol. 10 Issue 6, p870-870, 1p
Publication Year :
2020

Abstract

Alzheimer's disease is a neurodegenerative disorder for which there is a continuous search of drugs able to reduce or stop the cognitive decline. Beta-amyloid peptides are composed of 40 and 42 amino acids and are considered a major cause of neuronal toxicity. They are prone to aggregation, yielding oligomers and fibrils through the inter-molecular binding between the amino acid sequences (17–42) of multiple amyloid-beta molecules. Additionally, amyloid deposition causes cerebral amyloid angiopathy. The present study aims to identify, in the existing literature, natural plant derived products possessing inhibitory properties against aggregation. The studies searched proved the anti-aggregating effects by the thioflavin T assay and through behavioral, biochemical, and histological analysis carried out upon administration of natural chemical compounds to transgenic mouse models of Alzheimer's disease. According to our present study results, fifteen secondary metabolites from plants were identified which presented both evidence coming from the thioflavin T assay and transgenic mouse models developing Alzheimer's disease and six additional metabolites were mentioned due to their inhibitory effects against fibrillogenesis. Among them, epigallocatechin-3-gallate, luteolin, myricetin, and silibinin were proven to lower the aggregation to less than 40%. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
2218273X
Volume :
10
Issue :
6
Database :
Complementary Index
Journal :
Biomolecules (2218-273X)
Publication Type :
Academic Journal
Accession number :
144481839
Full Text :
https://doi.org/10.3390/biom10060870