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Stability of A?-fibril fragments in the presence of fatty acids.

ABSTRACT: We consider the effect of lauric acid on the stability of various fibril-like assemblies of A? peptides. For this purpose, we have performed molecular dynamics simulations of these assemblies either in complex with lauric acid or without presence of the ligand. While we do not observe a stabilizing effect on A?40 -fibrils, we find that addition of lauric acid strengthens the stability of fibrils built from the triple-stranded S-shaped A?42 -peptides considered to be more toxic. Or results may help to understand how the specifics of the brain-environment modulate amyloid formation and propagation.

SUBMITTER: Xi W 

PROVIDER: S-EPMC6798130 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Stability of Aβ-fibril fragments in the presence of fatty acids.

Xi Wenhui W   Vanderford Elliott K EK   Liao Qinxin Q   Hansmann Ulrich H E UHE  

Protein science : a publication of the Protein Society 20190911 11

We consider the effect of lauric acid on the stability of various fibril-like assemblies of Aβ peptides. For this purpose, we have performed molecular dynamics simulations of these assemblies either in complex with lauric acid or without presence of the ligand. While we do not observe a stabilizing effect on Aβ<sub>40</sub> -fibrils, we find that addition of lauric acid strengthens the stability of fibrils built from the triple-stranded S-shaped Aβ<sub>42</sub> -peptides considered to be more to  ...[more]