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Cover Feature: Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns (ChemBioChem 12/2019)
Author(s) -
Lin Ping,
Yao Hongwei,
Zha Jun,
Zhao Yibing,
Wu Chuanliu
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900327
Subject(s) - bicyclic molecule , peptide , chemistry , panning (audio) , folding (dsp implementation) , combinatorial chemistry , cystine , peptidomimetic , stereochemistry , cysteine , biochemistry , biology , engineering , enzyme , electrical engineering , paleontology , zoom , lens (geology)
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 3 10 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.