A new purified Lawsoniaside remodels amyloid-β fibrillation into a less toxic and non-amyloidogenic pathway.

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ID: 67166
2018
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Ranked #49 of 200 articles by views in International journal of biological macromolecules

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Abstract
Mounting evidence indicates soluble Aβ oligomers as the most toxic species causing neuronal death which leads to the onset and progression of Alzheimer disease (AD). Recently, it has been found that neurotoxic Aβ oligomers grow from monomeric species or arise following secondary nucleation by preformed mature fibrils. Thus, the use of natural compounds such as polyphenols to hinder the growth or to remodel Aβ fibrils is one of the most promising strategies for AD treatment. In our previous study, we showed that 1, 2, 4-trihydroxynaphthalene-2-O-β-d-glucopyranoside (THNG) inhibits Aβ aggregation during the early steps of the aggregation process, inhibits its conformational change to a β-sheet-rich structure, decreases its polymerization, inhibits its fibrillogenisis and reduces oxidative stress and aggregate cytotoxicity. Here, we used different spectroscopic and cell culture methods to check the effect of THNG on fibrils disaggregation. We showed that THNG binds to mature Aβ fibrils, rearrange their secondary structure, and remodels them into non-amyloid, less toxic, species by inhibiting their interaction with the plasma membrane. Our findings reveal that THNG is a good agent to remodel amyloid fibrils and could be used as a starting molecular scaffold to design new anti-AD drugs.
Reference Key
dhouafli2018ainternational Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Dhouafli, Zohra;Leri, Manuela;Bucciantini, Monica;Stefani, Massimo;Gadhoumi, Hamza;Mahjoub, Borhane;Ben Jannet, Hichem;Guillard, Jérôme;Tounsi, Moufida Saidani;Ksouri, Riadh;Hayouni, El Akrem;
Journal International journal of biological macromolecules
Year 2018
DOI
S0141-8130(18)30838-9
URL
Keywords
protein aggregation alzheimer disease aß(42) fibrils thng

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