Abstract
Molecular fibrils formed by aggregated amyloid peptides of various lengths and sequences are common pathological fingerprints of a large range of amyloid-related diseases, from type 2 diabetes to Parkinson’s, Huntington’s, or Alzheimer’s disease. Despite their tremendous biomedical importance, both the structural properties of peptide amyloid fibrils and the molecular mechanisms involved in their formation and propagation (i.e., the formation of nucleated seeds and fibril segments) remain notoriously difficult to investigate either experimentally or computationally (1–4).
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