Cover Feature: Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns (ChemBioChem 12/2019),ChemBioChem

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Cover Feature: Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns (ChemBioChem 12/2019)
ChemBioChem ( IF 2.6 ) Pub Date : 2019-05-21 , DOI: 10.1002/cbic.201900327
Ping Lin ₁ , Hongwei Yao ₁ , Jun Zha ₁ , Yibing Zhao ₁ , Chuanliu Wu ₁

Affiliation

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.

中文翻译：

封面功能：通过胱氨酸桥和脯氨酸转弯限制的有序和异构稳定的双环肽支架（ChemBioChem 12/2019）

封面特征图片显示了通过淘选自制的噬菌体展示肽库发现的双环肽。在他们的交流中，C。Wu等人。在2019年第12期的第1514页上（DOI：10.1002 / cbic.201800788）解释了他们如何发现和鉴定出一类具有有序但不规则二级结构的双环肽。这些肽具有保守的半胱氨酸/脯氨酸框架，用于将氧化折叠引导成由四个不规则匝和3 ₁₀螺旋组成的稠合双环结构。这项工作可以启发具有新结构的多环肽的设计和工程，并有益于新型蛋白质结合剂和治疗剂的开发。

更新日期：2019-05-21

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