Free cholesterol induces higher β-sheet content in Aβ peptide oligomers by aromatic interaction with Phe19.
Accumulating experimental evidence support an enhancing effect of free cholesterol on amyloid-beta (Aβ) aggregation. To probe the mechanisms of cholesterol-mediated Aβ aggregation, we applied all-atom molecular dynamic simulations on Aβ42 peptides in presence of free cholesterol. Several control sys...
Guardado en:
Autores principales: | Xiaolin Zhou, Jie Xu |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/bd04a645056041c888c328462e153e28 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The interaction between amyloid-β peptides and anionic lipid membranes containing cholesterol and melatonin.
por: Hannah Dies, et al.
Publicado: (2014) -
Interaction of β-sheet folds with a gold surface.
por: Martin Hoefling, et al.
Publicado: (2011) -
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
por: Rodrigo Cataldi, et al.
Publicado: (2021) -
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
por: Francesco Simone Ruggeri, et al.
Publicado: (2021) -
Nanoribbons self-assembled from short peptides demonstrate the formation of polar zippers between β-sheets
por: Meng Wang, et al.
Publicado: (2018)