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生物大分子结构模拟与精确测定:Peptide Mimics by Linear Arylamides: A Structural and Functional Diversity Test

  • 关键字: Peptide Mimics by Linear Arylamides 发布者:Zhan-Ting Li,* Jun-Li Hou and Chuang Li 发布时间:2009-03-02 21:03:39 点击数: 1816次

Acc. Chem. Res. 2008, 41, 1343-1353.
 
Peptide Mimics by Linear Arylamides: A Structural and Functional Diversity Test
 
Zhan-Ting Li,* Jun-Li Hou and Chuang Li
 
State Key Laboratory of Bio-Organic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China.
 
Abstract: Hydrogen-bonded oligoamide foldamers represent a large family of peptide mimics. This paper describes our recent efforts in creating arylamide-based foldamers whose compact conformations are stabilized by hydrogen bonding. Three classes of mimic structures, that is, folded or helical, zigzag, and straight oligomers, have been constructed by simply changing the positions of the substituents at the benzene rings in the backbones. Both amide and hydrazide units have been employed to construct the frameworks. To test their usefulness, these frameworks have been extensively modified and functionalized. The properties or functions of the mimic structures have been studied in discrete aspects, including acyclic molecular receptors, acceleration of anisole hydrolysis, facilitation of macrocyclization, assembly of homoduplex, molecular tweezers, nano networks and dynamic [2]catenanes. The results demonstrate that hydrogen bonded arylamide oligomers are a class of structurally unique peptide mimics. The folded oligomers themselves can be used as synthetic receptors for binding different guest molecules, while incorporation of different segments into one system can produce many desired shapes. In addition, all of the rigid frameworks can be readily functionalized at specific sites. We believe that our results have helped to open the door for some new chemistry in molecular recognition, self-assembly, and other related areas.