131177-58-7Relevant articles and documents
An In-tether Chiral Center Modulates the Helicity, Cell Permeability, and Target Binding Affinity of a Peptide
Hu, Kuan,Geng, Hao,Zhang, Qingzhou,Liu, Qisong,Xie, Mingsheng,Sun, Chengjie,Li, Wenjun,Lin, Huacan,Jiang, Fan,Wang, Tao,Wu, Yun-Dong,Li, Zigang
, p. 8013 - 8017 (2016)
The addition of a precisely positioned chiral center in the tether of a constrained peptide is reported, yielding two separable peptide diastereomers with significantly different helicity, as supported by circular dichroism (CD) and NMR spectroscopy. Single crystal X-ray diffraction analysis suggests that the absolute configuration of the in-tether chiral center in helical form is R, which is in agreement with theoretical simulations. The relationship between the secondary structure of the short peptides and their biochemical/biophysical properties remains elusive, largely because of the lack of proper controls. The present strategy provides the only method for investigating the influence of solely conformational differences upon the biochemical/biophysical properties of peptides. The significant differences in permeability and target binding affinity between the peptide diastereomers demonstrate the importance of helical conformation.
