12/14/14-Helix Formation in 2:1 /β-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints

详细信息    查看全文

• 作者：Dr. Baptiste Legrand ; Dr. Christophe André ; Laure Moulat ; Dr. Claude Didierjean ; Dr. Patrick Hermet ; Prof. Jean-Louis Bantignies ; Prof. Jean Martinez ; Dr. Muriel Amblard and Dr. Monique Calmè ; s
• 刊名：Chemistry - A European Journal
• 出版年：2016
• 出版时间：August 16, 2016
• 年：2016
• 卷：22
• 期：34
• 页码：11986-11990
• 全文大小：1856K
• ISSN：1521-3765

文摘

The highly constrained β-amino acid ABOC induces different types of helices in β urea and 1:1 α/β amide oligomers. The latter can adopt 11/9- and 18/16-helical folds depending on the chain length in solution. Short peptides alternating proteinogenic α-amino acids and ABOC in a 2:1 α/β repeat pattern adopted an unprecedented and stable 12/14/14-helix. The structure was established through extensive NMR, molecular dynamics, and IR studies. While the 1:1 α-AA/ABOC helices diverged from the canonical α-helix, the helix formed by the 9-mer 2:1 α/β-peptide allowed the projection of the α-amino acid side chains in a spatial arrangement according to the α-helix. Such a finding constitutes an important step toward the conception of functional tools that use the ABOC residue as a potent helix inducer for biological applications.