Helical secondary structures in 2:1 and 1:2 伪/纬-peptide foldamers

详细信息	查看全文 | 推荐本文 |

• 作者：Li Guo^a ; Weicheng Zhang^b ; Ilia A. Guzei^b ; Lara C. Spencer^b ; Samuel H. Gellman^b ; ^{gellman@chem.wisc.edu}
• 关键词：伪/纬-Peptide ; Foldamer ; Helical secondary structure ; 12-Helix
• 刊名：Tetrahedron
• 出版年：2012
• 期刊代码：107_00404020
• 类别：ch
• 出版时间：10 June, 2012
• 卷：68
• 期：23
• 页码：4413-4417
• 文件大小：418 K

摘要

Oligomers containing both 伪- and 纬-amino acid residues in a 1:1 alternating pattern have recently been shown by several research groups to adopt helical secondary structures. We have begun to explore the folding behavior of oligomers with different 伪-residue/纬-residue backbone patterns. Previously we reported that the 纬-amino acids bearing a cyclohexyl constraint at the C_尾-C_纬 bond and a variable side chain at C_伪 strongly promote a helical conformation containing 12-atom CO(i)鈰疕-N(i+3) hydrogen bonds for 1:1 伪:纬 backbones. Here we report synthesis and crystallographic analysis of 2:1 and 1:2 伪/纬-peptides that adopt CO(i)鈰疕-N(i+3) hydrogen-bonded helical conformations.