Abstract:
:Wild-type hen lysozyme has been converted from its soluble native state into highly organized amyloid fibrils. In order to achieve this conversion, conditions were chosen to promote partial unfolding of the native globular fold and included heating of low-pH solutions and addition of organic solvents. Two peptides derived from the beta-sheet region of hen lysozyme were also found to form fibrils very readily. The properties and morphologies of the amyloid fibrils formed by incubation either of the protein or the peptides are similar to those produced from the group of proteins associated with clinical amyloidoses. Fibril formation by hen lysozyme was substantially accelerated when aliquots of solutions in which fibrils of either one of the peptides or the full-length protein had previously formed were added to fresh solutions of the protein, revealing the importance of seeding in the kinetics of fibril formation. These findings support the proposition that the beta-domain is of particular significance in the formation of fibrils from the full-length protein and suggest similarities between the species giving rise to fibril formation and the intermediates formed during protein folding.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Krebs MR,Wilkins DK,Chung EW,Pitkeathly MC,Chamberlain AK,Zurdo J,Robinson CV,Dobson CMdoi
10.1006/jmbi.2000.3862keywords:
subject
Has Abstractpub_date
2000-07-14 00:00:00pages
541-9issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(00)93862-2journal_volume
300pub_type
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