Coarse‐grained and All‐atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

Abstract

AbstractAlzheimer's disease is the most common neurodegenerative disease. Experiments and computer simulations can complement one another to provide a full and in‐depth understanding of many aspects in the amyloid field at the atomistic level. Here, we review results of our coarse‐grained and all‐atom simulations in aqueous solution aimed at determining: 1) early aggregation steps of short linear peptides; 2) nucleation size number; 3) solution structure of the Aβ1–40/Aβ1–42 wild‐type dimers; 4) impact of FAD (familial forms of Alzheimer's disease) mutations on the structure of Aβ1–40/Aβ1–42 dimers; and 5) impact of protective mutations on the structure of Aβ1–40/Aβ1–42 dimers.