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Journal of Biochemistry Advance Access published online on April 16, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn051
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© 2008 The Japanese Biochemical Society

Rapid Communication

Requirement of Ala residues at g position in heptad sequence of {alpha}-helix-forming peptide for formation of fibrous structure

Gaku Aokia, Toyo K. Yamadaa, Mayu Ariib, Shuichi Kojimab and Tadashi Mizoguchia

aDepartment of Physics and bInstitute for Biomolecular Science, Faculty of Science, Gakushuin University, Mejiro, Tokyo 171-8588, Japan

*To whom correspondence should be addressed: Prof. Shuichi Kojima. Institute for Biomolecular Science, Faculty of Science, Gakushuin University, Mejiro 1-5-1, Toshima-ku, Tokyo 171-8588, Japan, Tel : +81-3-3986-0221, ext.6505, Fax +81-3-5992-1034, E-mail address: shuichi.kojima{at}gakushuin.ac.jp

Received March 4, 2008; Accepted April 8, 2008


  Abstract

One feature of the {alpha}3-peptide, which has the amino acid sequence of (Leu-Glu-Thr-Leu-Ala-Lys-Ala)3, that distinguishes it from many other {alpha}-helix-forming peptides is its ability to form fibrous assemblies that can be observed by transmission electron microscopy. In this study, the effects of Ala->Gln substitution at the e (5th) or g (7th) position in the above heptad sequence of the {alpha}3-peptide on the formation of {alpha}-helix and fibrous assemblies were investigated by circular dichroism spectral measurement and atomic force microscopy. The 5Q{alpha}3-peptide obtained by Ala->Gln substitution at the e position of the {alpha}3-peptide was found to form very short fibrils with long-elliptical shape, whereas the 7Q{alpha}3-peptide with Gln residues at the g position lost its ability to form such assemblies, in spite of {alpha}-helix formation in both peptides; the stabilities of both peptides decreased. These results indicate that Ala residues at the g position in the heptad sequence of the {alpha}3-peptide are key residues for the formation of fibrous assemblies, which may be due to hydrophobic interactions between {alpha}-helical bundle surfaces.

Key Words: {alpha}-helix, atomic force microscopy, circular dichroism spectra, fiber formation, heptad sequence


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