Dual In-Tether Chiral Centers Modulate Peptide Helicity

作者：Hu, Kuan; Sun, Chengjie; Yu, Mengying; Li, Wenjun; Lin, Huacan; Guo, Jialin; Jiang, Yixiang; Lei, Chengxiang; Li, Zigang^*

来源：Bioconjugate Chemistry, 2017, 28(5): 1537-1543.

DOI：10.1021/acs.bioconjchem.7b00171

• RING-CLOSING METATHESIS
• TARGET BINDING-AFFINITY
• SIDE-CHAIN CYCLIZATION
• STAPLED PEPTIDES
• ENANTIOSELECTIVE SYNTHESIS
• SECONDARY STRUCTURE
• SULFOXIDE
• PROTEIN
• MACROCYCLIZATION
• CONFORMATION

The facile chemical modification on the peptide cross-linking moiety is an important strategy for improving the physicochemical properties of a peptide. Herein, peptides were constrained into helical conformations via the synergistic effects of dual in-tether chiral centers. A pentapeptide minimalistic model was used to determine the correlation between the absolute configurations of the dual in-tether chiral centers and the secondary structures of the peptides. This strategy provides an on-tether modification site that does not interrupt the secondary structure of the peptide.

• 出版日期2017-5
• 单位北京大学; 北京大学深圳研究生院