Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

David R. Booth, Margaret Sunde, Vittorio Bellotti, Carol V. Robinson, Winston L. Hutchinson, Paul E. Fraser, Philip N. Hawkins, Christopher M. Dobson, Sheena E. Radford, Colin C. F. Blake and Mark B. Pepys
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David R. Booth: Royal Postgraduate Medical School, Hammersmith Hospital
Margaret Sunde: Oxford Centre for Molecular Sciences, University of Oxford
Vittorio Bellotti: Royal Postgraduate Medical School, Hammersmith Hospital
Carol V. Robinson: Oxford Centre for Molecular Sciences, University of Oxford
Winston L. Hutchinson: Royal Postgraduate Medical School, Hammersmith Hospital
Paul E. Fraser: University of Toronto
Philip N. Hawkins: Royal Postgraduate Medical School, Hammersmith Hospital
Christopher M. Dobson: Oxford Centre for Molecular Sciences, University of Oxford
Sheena E. Radford: Oxford Centre for Molecular Sciences, University of Oxford
Colin C. F. Blake: Oxford Centre for Molecular Sciences, University of Oxford
Mark B. Pepys: Royal Postgraduate Medical School, Hammersmith Hospital

Nature, 1997, vol. 385, issue 6619, 787-793

Abstract: Abstract Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-β fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

Date: 1997
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DOI: 10.1038/385787a0

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