@article{oai:nagasaki-u.repo.nii.ac.jp:00004159,
 author = {Demizu, Yosuke and Yamashita, Hiroko and Misawa, Takashi and Doi, Mitsunobu and Tanaka, Masakazu and Kurihara, Masaaki},
 issue = {3},
 journal = {Chemical and Pharmaceutical Bulletin},
 month = {Mar},
 note = {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 righthanded (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. c 2015 The Pharmaceutical Society of Japan α -aminoisobutyric acid; peptide; conformation; helical structure., Chemical and Pharmaceutical Bulletin, 63(3), pp.218-224; 2015},
 pages = {218--224},
 title = {Effects of D-Leu Residues on the Helical Secondary Structures of L-Leu-Based Nonapeptides},
 volume = {63},
 year = {2015}
}