Many proteins can enter an amyloid state, where they aggregate into long, unbranched fibrils characterized by beta sheets.  This amyloid state is closely associated with disease, one of the most well-known being Alzheimer’s, a disorder linked to aggregation of the amyloid beta (Aβ) peptide in the brain.  Recent data indicate that soluble oligomers, which form earlier than mature fibrils, may be the true toxic species in many neurodegenerative diseases.  Because these oligomers are structurally transient and heterogeneous, they are difficult to characterize experimentally, especially in atomistic detail.  I will discuss our efforts using molecular dynamics simulations to characterize monomers and oligomers in different amyloid systems, including Aβ.

Characterizing amyloid beta monomers and oligomers with long-timescale molecular dynamics simulations

2019 Spring National Meeting

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