Nature Communications (Jan 2019)
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
- 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
Affiliations
- Ryan Limbocker
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Sean Chia
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Francesco S. Ruggeri
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Michele Perni
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Roberta Cascella
- Department of Experimental and Clinical Biomedical Science, University of Florence
- Gabriella T. Heller
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Georg Meisl
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Benedetta Mannini
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Johnny Habchi
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Thomas C. T. Michaels
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Pavan K. Challa
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Minkoo Ahn
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Samuel T. Casford
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Nilumi Fernando
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Catherine K. Xu
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Nina D. Kloss
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Samuel I. A. Cohen
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Janet R. Kumita
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Cristina Cecchi
- Department of Experimental and Clinical Biomedical Science, University of Florence
- Michael Zasloff
- MedStar-Georgetown Transplant Institute, Georgetown University School of Medicine
- Sara Linse
- Department of Biochemistry and Structural Biology, Lund University
- Tuomas P. J. Knowles
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Fabrizio Chiti
- Department of Experimental and Clinical Biomedical Science, University of Florence
- Michele Vendruscolo
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- Christopher M. Dobson
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge
- DOI
- https://doi.org/10.1038/s41467-018-07699-5
- Journal volume & issue
-
Vol. 10,
no. 1
pp. 1 – 13
Abstract
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.
