期刊
ChemBiochem
标题Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns
作者
Ping Lin, Hongwei Yao, Jun Zha, Yibing Zhao, Chuanliu Wu
摘要
The cover feature picture shows a bicyclic peptide discovered by panning a home‐made phage display peptide library. In their communication, C. Wu et al. on page 1514 in Issue 12, 2019 (DOI: 10.1002/cbic.201800788) explain how they have discovered and identified a class of bicyclic peptides with ordered but irregular secondary structures. These peptides have a conserved cysteine/proline framework for directing the oxidative folding into a fused bicyclic structure consisting of four irregular turns and a 310 helix. This work could inspire the design and engineering of multicyclic peptides with new structures and benefit the development of novel protein binders and therapeutics.
原文链接
https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201900327