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- Title
An In-tether Chiral Center Modulates the Helicity, Cell Permeability, and Target Binding Affinity of a Peptide.
- Authors
Kuan Hu; Hao Geng; Qingzhou Zhang; Qisong Liu; Mingsheng Xie; Chengjie Sun; Wenjun Li; Huacan Lin; Fan Jiang; Tao Wang; Yun-Dong Wu; Zigang Li
- Abstract
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.
- Subjects
HELICITY (Chemistry); CHIRALITY; PERMEABILITY measurement; CHEMICAL affinity; CHIRAL centers; GENETICS
- Publication
Angewandte Chemie International Edition, 2016, Vol 55, Issue 28, p8013
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201602806