Molecular dissection of the core of lysozyme amyloid fibril

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Lysozyme is one of the amyloidogenic proteins. Here, by using hen lysozyme disulfide-deficient variants and synthetic peptides covering specific residue positions, we investigated the mechanism of the core formation of lysozyme amyloid fibrils. Peptide regions involved in the core formation in normal monomolecular folding are also involved in misfolding and core formation of lysozyme amyloid fibrils. Specifically, absence of a structure which could interact and successfully accept a highly beta-aggregating structure in normal folding reaction leads to misfolding and fibrillogenesis through intermolecular beta-aggregation.