期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 16, 期 42, 页码 7947-7958出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8ob02279h
关键词
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Unlike the extensively investigated relationship between the peptide -bend ribbon and its prototypical 3(10)-helix conformation, the corresponding relationship between the narrower -bend ribbon and its regular -helix counterpart still remains to be studied, as the latter 3D-structures have not yet been experimentally authenticated. In this paper, we describe the results of the first characterization, both in the crystal state and in solution, of the -bend ribbon conformation using X-ray diffraction and FT-IR absorption, electronic CD and 2D-NMR spectroscopies applied to an appropriate set of synthetic, homo-chiral, sequential dipeptide oligomers based on (S)-Ala and the known -bend inducer, C-tetrasubstituted, N-alkylated -amino acid residue (S)-C-methyl-azetidine-carboxylic acid.
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