Comparison of Oct-2-enyl and Oct-4-enyl Staples for Their Formation and α-Helix Stabilizing Effects

Bulletin of the Korean chemical society

Jiyeon Yoo¹  Thanh K. Pham¹  Young-Woo Kim¹ 

关键词: -Helix;    Stapled peptides;    Ring-closing metathesis;    Protease resistance;    Peptide drugs;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

The all-hydrocarbon i,i+4 stapling system using an oct-4-enyl crosslink is one of the most widely employed chemical tools to stabilize an α-helical conformation of a short peptide. This crosslinking system has greatly extended our ability to modulate intracellular protein-macromolecule interactions. The helix-inducing property of the i,i+4 staple has shown to be highly dependent on the length and the stereochemistry of the oct-4-enyl crosslink. Here we show that changing the double bond position within the i,i+4 staple has a considerable impact not only on the formation of the crosslink but also on α-helix induction. The data further increases the understanding of the structure-activity relationships of this valuable chemical tool.

【 授权许可】

Unknown