Recent advances in high-resolution structural studies of protein amyloids have revealed parallel in-register cross-β-sheets with periodic arrays of closely spaced identical residues. What do these structures tell us about the mechanisms of action of common amyloid-promoting factors, such as heparan sulfate (HS), nucleic acids, polyphosphates, anionic phospholipids, and acidic pH?
Keywords: amyloid nucleation; cross-β-sheet; electrostatic interactions; flexible docking; heparan sulfate; periodic polyanions.
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