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Coralie Di Scala, Jean-Denis Troadec, Clément Lelièvre, Nicolas Garmy, Jacques Fantini and Henri Chahinian Mechanism of cholesterol-assisted oligomeric channel formation by a short Alzheimer β-amyloid peptide Journal of Neurochemistry 128

Version of Record online: 28 AUG 2013 | DOI: 10.1111/jnc.12390

Thumbnail image of graphical abstract

Aβ22-35 peptide, which encompasses the cholesterol binding domain of Aβ, induces a specific increase of Ca2+ level in neural cells. Double mutations V24G/K28G and N27R/K28R modify cholesterol binding and abrogate channels formation. Molecular dynamic simulations suggest that cholesterol induces a tilted α-helical peptide topology facilitating the formation of annular octameric channels, as schematically shown in the graphic (with a hydrogen bond shown in green for two vicinal peptides). Overall, the data give insights into the role of cholesterol in amyloid channel formation and open up new therapeutic options for Alzheimer's disease.

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