Conformational studies on peptides having chiral five-membered ring amino acid with two azido or triazole functional groups within the sequence of Aib residues

TETRAHEDRON

卷:70

Article

Oba, Makoto¹  Kawabe, Naomi²  Takazaki, Hiroomi²  Demizu, Yosuke³  Doi, Mitsunobu⁴  Kurihara, Masaaki³  Suemune, Hiroshi²  Tanaka, Masakazu¹ 

[1] Nagasaki Univ, Grad Sch Biomed Sci, Nagasaki 8528521, Japan

[2] Kyushu Univ, Grad Sch Pharmaceut Sci, Fukuoka 8128582, Japan

[3] Natl Inst Hlth Sci, Div Organ Chem, Tokyo 1588501, Japan

[4] Osaka Univ Pharmaceut Sci, Osaka 5691094, Japan

关键词: Amino acids;    Chirality;    Conformation analysis;    Helical structures;    Peptides;   

DOI  :  10.1016/j.tet.2014.09.086

来源: Elsevier

【 摘 要 】

The chiral cyclic alpha,alpha-disubstituted alpha-amino acid, (3R,4R)-1-amino-3,4-diazido-1-cyclopentanecarboxylic acid [(R,R)-Ac-5C(dN3)], was introduced into achiral alpha-aminoisobutyric acid (Aib) peptides. The azido groups of (R,R)-Ac-5C(dN3) in the peptides were efficiently converted into 1,2,3-triazole functional groups. FTIR, H-1 NMR, and CD spectra revealed that the dominant conformations of all peptides in solution were 3(10)-helical structures without controlling the helical-screw sense. X-ray crystallographic analyses of peptides containing (R,R)-Ac-5C(dN3) showed that both the right-handed (P) and left-handed (M) 3(10)-helical structures were present in the crystal state. (C) 2014 Elsevier Ltd. All rights reserved.

【 授权许可】

Free