PUBLICATION

Amylovis-201 is a new dual-target ligand, acting as an anti-amyloidogenic compound and a potent agonist of the σ1 chaperone protein

Authors
García-Pupo, L., Crouzier, L., Bencomo-Martínez, A., Meunier, J., Morilleau, A., Delprat, B., Carrazana, M.S., Menéndez Soto Del Valle, R., Maurice, T., Rodríguez-Tanty, C.
ID
ZDB-PUB-241114-21
Date
2024
Source
Acta pharmaceutica Sinica. B   14: 434543594345-4359 (Journal)
Registered Authors
Keywords
Alzheimer's disease, Amyloid-β aggregation, Drug discovery, Learning and memory, Molecular modelisation, Neuroprotection, Zebrafish model, σ1 receptor
MeSH Terms
none
PubMed
39525570 Full text @ Acta Pharm Sin B
Abstract
The aggregation of Amyloid-β (Aβ) peptides is associated with neurodegeneration in Alzheimer's disease (AD). We previously identified novel naphtalene derivatives, including the lead compound Amylovis-201, able to form thermodynamically stable complexes with Aβ species, peptides and fibrils. As the drug showed a chemical scaffold coherent for an effective interaction with the σ1 receptor chaperone and as σ1 agonists are currently developed as potent neuroprotectants in AD, we investigated the pharmacological action of Amylovis-201 on the σ1 receptor. We report that Amylovis-201 is a potent σ1 agonist by several in silico, in vitro and in vivo assays and that its anti-amnesic and neuroprotective effects involve a pharmacological action at σ1 receptors. Furthermore, we show for the first time that classical σ1 receptor agonist (PRE-084), and antagonist (NE-100) are able to interact and disaggregate Aβ25-35 fibrils. Interestingly, Amylovis-201 was the only compound inhibiting Aβ25-35 aggregates formation. Our results therefore highlight a dual action of Amylovis-201 as anti-aggregating agent and σ1 receptor agonist that could be highly effective in long-term treatment against neurodegeneration in AD.
Genes / Markers
Figures
Show all Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping