流动化学促进β-肽的高效合成：主链拓扑结构与螺旋形成。
Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation.
机构信息
Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., H-6720 Szeged, Hungary.
出版信息
Chem Commun (Camb). 2019 Mar 7;55(21):3061-3064. doi: 10.1039/c8cc10147g.
PMID:30720807
Abstract
Enantiodiscriminative helix formation was observed for β-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.
摘要
β-肽 H14 螺旋形成了对映体选择性的螺旋结构。这种观察结果是由 H-O 原子的同平面取向引起的，这种取向比 H-H 相互作用更不利。1,2 H-O 相互作用导致螺旋结构的破坏。在主链中引入双键会排除螺旋结构的形成。
Zotero 插件