Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

Transient oligomeric species of the amyloid-β peptide (Aβ42) have been identified as key pathogenic agents in Alzheimer’s disease. Here the authors find that the aminosterol trodusquemine enhances Aβ42 aggregation and suppresses Aβ42-induced toxicity by displacing oligomers from cell membranes....

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Autores principales: Ryan Limbocker, Sean Chia, Francesco S. Ruggeri, Michele Perni, Roberta Cascella, Gabriella T. Heller, Georg Meisl, Benedetta Mannini, Johnny Habchi, Thomas C. T. Michaels, Pavan K. Challa, Minkoo Ahn, Samuel T. Casford, Nilumi Fernando, Catherine K. Xu, Nina D. Kloss, Samuel I. A. Cohen, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Sara Linse, Tuomas P. J. Knowles, Fabrizio Chiti, Michele Vendruscolo, Christopher M. Dobson
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Science
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Acceso en línea:https://doaj.org/article/e4aca3eea6e44315b03de5b6488da79d
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Sumario:Transient oligomeric species of the amyloid-β peptide (Aβ42) have been identified as key pathogenic agents in Alzheimer’s disease. Here the authors find that the aminosterol trodusquemine enhances Aβ42 aggregation and suppresses Aβ42-induced toxicity by displacing oligomers from cell membranes.

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