Oligomer stability of Amyloid-$\beta$ (A$\beta$) 25-35 : A Dissipative Particle Dynamics study

Alzheimer's disease is strongly associated with an accumulation of Amyloid-$\beta$ (A$\beta$) peptide plaques in the human brain. A$\beta$ is a 43 residues long intrinsically disordered peptide and has a strong tendency to form aggregates. Evidence accumulates that A$\beta$ acts toxic to the neurons in the brain through the formation of small soluble oligomers. A$\beta$ 25-35 is the smallest fragment of A$\beta$ which still retains its toxicity and its ability to form extended fibrils. In this talk we will present the results from simulations of aggregation of up to 100 A$\beta$ 25-35 peptides using a novel polarizable coarse-grained protein model in combination with Dissipative Particle Dynamics.