The .ALPHA.-helical conformation of the Aib-containing oligopeptide, Boc-(Leu3-Aib)2-OBzl.

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概要

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• The octapeptide Boc–(Leu<SUB>3</SUB>–Aib)<SUB>2</SUB>–OBzl crystallizes in the space group <I>P</I>2<SUB>1</SUB>, with <I>a</I>=11.450(2), <I>b</I>=27.915(7), <I>c</I>=11.255(2) Å, β=116.95(1)°, and <I>Z</I>=2. The crystal structure has been solved by direct methods and refined to an <I>R</I> value of 0.08. The peptide back-bone, except for the C-terminal Aib residue, folds into a right-handed α-helical conformation, stabilized by four intramolecular (5→1) hydrogen bonds and two intermolecular hydrogen bonds between molecules related by the 2<SUB>1</SUB> symmetry along the <I>b</I> direction. In order to determine the helical conformation definitively, the helical parameters (unit height <I>h</I> and unit twist θ) at each amino-acid residue were derived from the bond lengths, bond angles, and torsional angles of the peptide main chain. The average values of these parameters for seven residues (<I>h</I>=1.57 Å and θ=99.0°) showed much better agreement with those for an α-helix (<I>h</I>=1.5 Å and θ=100°) rather than with those for a 3<SUB>10</SUB>-helix (<I>h</I>=2.0 Å and θ=120°). Peptide helices are arranged in columns in head-to-tail fashion. These columns are packed in parallel with respect to their helical direction. Between neighbouring chains of helices only hydrophobic contacts are found.

• 公益社団法人 日本化学会の論文

著者

• TANAKA Nobuo

  Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology

• Okuyama Kenji

  Faculty Of Technology Tokyo University Of Agriculture & Technology

• Doi Masamitsu

  Faculty of Technology, Tokyo University of Agriculture and Technology

• Narita Mitsuaki

  Faculty of Technology, Tokyo University of Agriculture and Technology

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