Elongation in a .BETA.-Structure Promotes Amyloid-Like Fibril Formation of Human Lysozyme.

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概要

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• To understand the mechanism of amyloid fibril formation of a protein, we examined wild-type and three mutant human lysozymes containing both amyloidogenic and nonamyloidogenic proteins: 156T (amyloidogenic); EAEA, which has four additional residues (Glu-Ala-Glu-Ala-) at the N-terminus located on a β-structure; and EAEA-156T, which is an 156T mutant of EAEA. All formed amyloid-like fibrils through an in the increase contents of α-helix with increasing concentration of ethanol. The order of propensity for amyloid-like fibril formation in highly concentrated ethanol solution is EAEA-156T> EAEA> 156T> wild-type. This order is almost the reverse of the order of conformational stability of these proteins, wild-type>EAEA> I56T> EAEA-156T. The important views in this work are as follows. (i) Artificially modified proteins formed amyloid fibrils in vitro. This means that amyloid formation is a generic property of polypeptide chains. (ii) The amyloidogenic mutation 11e56 to Thr caused the destabiliza-tion and promoted fibril formation in the wild-type and EAEA human lysozymes, indi-cating that instability facilitates amyloid formation. (iii) The mutant protein EAEA human lysozyme had higher propensity for fibril formation than the amyloidogenic mutant protein, indicating that amyloid formation is controlled not only by stability but also by other factors. In this case, appending polypeptide chains to a β-structure accel-erated amyloid formation.

• 社団法人 日本生化学会の論文

著者

• YUTANI Katsuhide

  Institute for Protein Research, Osaka University

• Yamagata Yuriko

  Graduate School Of Pharmaceutical Sciences Kumamoto University

• Takano Kazufumi

  Institute For Protein Research Osaka University

• Maki Saori

  Protonic Nanomachine Project Erato Jst

• Goda Shuichiro

  Institute For Protein Research Osaka University

• Namba Keiichi

  Protonic Nano Machine Group Graduate School Of Frontier Biosciences Osaka University

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