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Stability of Aβ‐fibril fragments in the presence of fatty acids
Author(s) -
Xi Wenhui,
Vanderford Elliott K.,
Liao Qinxin,
Hansmann Ulrich H. E.
Publication year - 2019
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3719
Subject(s) - lauric acid , fibril , molecular dynamics , chemistry , amyloid fibril , biophysics , amyloid (mycology) , fatty acid , ligand (biochemistry) , biochemistry , receptor , computational chemistry , amyloid β , biology , medicine , inorganic chemistry , disease , pathology
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 40 ‐fibrils, we find that addition of lauric acid strengthens the stability of fibrils built from the triple‐stranded S‐shaped Aβ 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.