Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Amyloid Fibril Formation of Hen Lysozyme Depends on the Instability of the C-Helix (88-99)
Akihito HARADAHiroyuki AZAKAMIAkio KATO
著者情報
キーワード: amyloid, α-helix, lysozyme
ジャーナル フリー

2008 年 72 巻 6 号 p. 1523-1530

詳細
抄録
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.
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© 2008 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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