Abstract
Aggregation of Aβ peptides is related to the onset of Alzheimer's disease, but the molecular mechanism of the Aβ fibril formation is still poorly understood. Recently, we have studied the thermodynamics and free energy landscape of Aβ fibril growth using a hexamer system of Aβ10-40 peptides by replica exchange molecular dynamics simulations and atomistic implicit solvent model. The system consisted of four peptides forming a fibril fragment and two incoming peptides binding to the fibril edge. We have demonstrated that deposition of the peptides onto the fibril follows the “dock-lock” mechanism.
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