Effects of D-Leu Residues on the Helical Secondary Structures of L-Leu-Based Nonapeptides

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  • Demizu Yosuke
    Division of Organic Chemistry, National Institute of Health Sciences
  • Yamashita Hiroko
    Division of Organic Chemistry, National Institute of Health Sciences Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Misawa Takashi
    Division of Organic Chemistry, National Institute of Health Sciences
  • Doi Mitsunobu
    Osaka University of Pharmaceutical Sciences
  • Tanaka Masakazu
    Graduate School of Biomedical Sciences, Nagasaki University
  • Kurihara Masaaki
    Division of Organic Chemistry, National Institute of Health Sciences Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology

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The influence of D-Leu residues on the helical structures of L-Leu-based-nonapeptides was investigated. Specifically, the preferred conformations of four diastereomeric nonapeptides, Boc-(L-Leu-L-Leu-Aib)3-OMe (1); Boc-(L-Leu-L-Leu-Aib)2-L-Leu-D-Leu-Aib-OMe (2), which contained one D-Leu residue; Boc-L-Leu-D-Leu-Aib-L-Leu-L-Leu-Aib-L-Leu-D-Leu-Aib-OMe (3), which contained two D-Leu residues; and Boc-(L-Leu-D-Leu-Aib)3-OMe (4), were analyzed in solution and in the crystalline state. Peptide 1 formed a right-handed (P) 310-helix in solution. Peptides 2 and 3 both formed (P) 310-helices in solution and (P) α-helices in the crystalline state. Peptide 4 formed a (P) α-helix both in solution and in the crystalline state.

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