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Journal of Biochemistry Advance Access originally published online on April 16, 2008
Journal of Biochemistry 2008 144(1):15-19; 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 Aoki1, Toyo K. Yamada1, Mayu Arii2, Shuichi Kojima2,* and Tadashi Mizoguchi1

1Department of Physics; and 2Institute for Biomolecular Science, Faculty of Science, Gakushuin University, Mejiro, Tokyo 171-8588, Japan

*To whom correspondence should be addressed. Tel: +81-3-3986-0221, ext. 6505, Fax: +81-3-5992-1034, E-mail: 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, fibre formation, heptad sequence

Abbreviations: AFM, atomic force microscopy; TEM, transmission electron microscopy


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