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Article

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.

Biophysical chemistry - 1 Apr 2021

Vettore Nicola, Moray Joël, Brans Alain, Herman Raphaël, Charlier Paulette, Kumita Janet R, Kerff Frédéric, Dobson Christopher M, Dumoulin Mireille

Abstract excerpt

The accumulation in vital organs of amyloid fibrils made of mutational variants of lysozyme (HuL) is associated with a human systemic amyloid disease. The detailed comparison of the in vitro properties of the I56T and D67H amyloidogenic variants to those of the T70N non-amyloidogenic variant and the wild-type (WT) protein suggested that the deposition of large amounts of aggregated disease-related lysozyme...

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Identifiers

PMID: 33640796
DOI: 10.1016/j.bpc.2021.106563

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