Alzheimer’s disease(AD) is well-known as a neurodegenerative disorder characterized by extracellular senile plaques in brain. The fibrillar aggregation of amyloid-β (Aβ) peptides plays an essential role in the pathology of AD. Previous experimental work points out that fatty acids such as lauric acid could induce oligomerization of Aβ42. We use docking methods to predict the target binding sites of the lauric acid for a certain model of Aβ42 oligomers. Then we study the interaction between Aβ peptides and lauric acid with atomistic molecular dynamics(MD) simulation and try to reveal the influence of ligands for Aβ42 oligomers and the corresponding molecular mechanism. The reasonable binding sites suggest the negative-charged ligands might influence the Lysine residues on Aβ42 oligomers. Meanwhile, the stability of Aβ42 oligomers is increased significantly when the ratio of Aβ42 peptide to lauric acid is 1:1.
Basal knowledge of biochemistry and the technology of programming and know how to use software such as VMD and gromacs.