Amyloid fibril formation of hen lysozyme depends on the instability of the C-helix (88-99)

Akihito Harada, Hiroyuki Azakami, Akio Kato

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Stable and unstable mutant lysozymes in long helices B and C were constructed to evaluate the effect of the helices on amyloid fibril formation at pH 2. Stable mutant N27D and unstable mutant K33D in the B-helix did not change in amyloid fibril formation. In contrast, stable mutant N93D and unstable mutant K97D in the C-helix showed big differences in behavior as to amyloid fibril formation. Stable mutant N93D showed a longer lag phase of aggregation and suppressed the amyloid fibril formation, whereas unstable mutant K97D showed a shorter lag phase of aggregation and accelerated amyloid fibril formation. These results suggest that the long C-helix is involved mainly in the α-helix to β-sheet transition during amyloid formation of lysozyme.

Original languageEnglish
Pages (from-to)1523-1530
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume72
Issue number6
DOIs
Publication statusPublished - Jul 1 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Amyloid fibril formation of hen lysozyme depends on the instability of the C-helix (88-99)'. Together they form a unique fingerprint.

  • Cite this