Chem. Pharm. Bull.

Chem. Pharm. Bull., 55(5),840-842, May 2007

Communications to the Editor

Controlling 3₁₀-Helix and α-Helix of Short Peptides in the Solid State

Yosuke DEMIZU,^a Masakazu TANAKA,^^,a Masanobu NAGANO,^a Masaaki KURIHARA,^b Mitsunobu DOI,^c Tokumi MARUYAMA,^d and Hiroshi SUEMUNE^^,a

^a Graduate School of Pharmaceutical Sciences, Kyushu University; 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan: ^b Division of Organic Chemistry, National Institute of Health Sciences; Tokyo 158-8501, Japan: ^c Osaka University of Pharmaceutical Sciences; Osaka 569-1094, Japan: and ^d Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University; Kagawa 769-2193, Japan. * To whom correspondence should be addressed. e-mail: mtanaka@phar.kyushu-u.ac.jp;

L-Leu hexapeptide containing α-aminoisobutyric acid (Aib) forms a right-handed (P) 3₁₀-helix, whereas that containing cyclic α,α-disubstituted amino acid Ac₅c^dOM assumes a right-handed (P) α-helix in the solid state.

Key words α,α-disubstituted amino acid; peptide; helix; conformation; secondary structure

Communications to the Editor

Controlling 310-Helix and α-Helix of Short Peptides in the Solid State

Yosuke DEMIZU,a Masakazu TANAKA,*,a Masanobu NAGANO,a Masaaki KURIHARA,b Mitsunobu DOI,c Tokumi MARUYAMA,d and Hiroshi SUEMUNE*,a

Controlling 3₁₀-Helix and α-Helix of Short Peptides in the Solid State

Yosuke DEMIZU,^a Masakazu TANAKA,^^,a Masanobu NAGANO,^a Masaaki KURIHARA,^b Mitsunobu DOI,^c Tokumi MARUYAMA,^d and Hiroshi SUEMUNE^^,a