Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class, can modulate the aggregation of the amyloid-β pe...

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Bibliographic Details
Main Authors: Ryan Limbocker, Roxine Staats, Sean Chia, Francesco S. Ruggeri, Benedetta Mannini, Catherine K. Xu, Michele Perni, Roberta Cascella, Alessandra Bigi, Liam R. Sasser, Natalie R. Block, Aidan K. Wright, Ryan P. Kreiser, Edward T. Custy, Georg Meisl, Silvia Errico, Johnny Habchi, Patrick Flagmeier, Tadas Kartanas, Jared E. Hollows, Lam T. Nguyen, Kathleen LeForte, Denise Barbut, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Tuomas P. J. Knowles, Christopher M. Dobson, Fabrizio Chiti, Michele Vendruscolo
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-06-01
Series:Frontiers in Neuroscience
Subjects:
protein misfolding diseases
amyloid-β
Alzheimer’s disease
α-synuclein
Parkinson’s disease
oligomers
Online Access:https://www.frontiersin.org/articles/10.3389/fnins.2021.680026/full

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https://www.frontiersin.org/articles/10.3389/fnins.2021.680026/full

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