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

作者：Harada Akihito; Azakami Hiroyuki; Kato Akio^*

来源：Bioscience Biotechnology and Biochemistry, 2008, 72(6): 1523-1530.

DOI：10.1271/bbb.80032

• amyloid
• alpha-helix
• lysozyme

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 a-helix to beta-sheet transition during amyloid formation of lysozyme.

• 出版日期2008-6