Chinese Journal of Organic Chemistry ›› 2020, Vol. 40 ›› Issue (6): 1473-1483.DOI: 10.6023/cjoc201911030 Previous Articles     Next Articles


黄净a, 杨毅华b, 冯娟b, 李军章b, 刘守信a   

  1. a 河北科技大学 省部共建国家重点实验室培育基地-河北省药用分子化学重点实验室 河北石家庄 050018;
    b 河北科技大学化学与制药工程学院 河北石家庄 050018
  • 收稿日期:2019-11-25 修回日期:2020-01-15 发布日期:2020-03-11
  • 通讯作者: 杨毅华, 刘守信;
  • 基金资助:

Research Progress on cis-/trans-Isomerization of Cyclic Peptide

Huang Jinga, Yang Yihuab, Feng Juanb, Li Junzhangb, Liu Shouxina   

  1. a State Key Laboratory Breeding Base, Hebei Key Laboratory of Molecular Chemistry for Drug, Hebei University of Science & Technology, Shijiazhuang, Hebei 050018;
    b College of Chemical and Pharmaceutical Engineering, Hebei University of Science & Technology, Shijiazhuang, Hebei 050018
  • Received:2019-11-25 Revised:2020-01-15 Published:2020-03-11
  • Supported by:
    Project supported by the National Basic Research Program of China (Nos. 2011CB512007, 2012CB723501), and the National Natural Science Foundation of China (Nos. 30472074, 30873139).

This paper focuses on cis-/trans-conformational interchanges of amide bonds in cyclic peptides that contain N-unsubstituted amino acids, N-methylated amino acids, and prolines. Conformational preferences of such cyclic peptides and their analogs are discussed. Proline has strong influences on the conformation due to the five-membered cyclic structure. N-Methylation not only increased the steric hindrance, but also led to increased population of cis-conformation of the amide bond.

Key words: cis-/trans-structure, cis-/trans-isomerization, cyclic peptide, bioactivity