A phage display-based strategy for the de novo creation of disulfide-constrained and isomer-free bicyclic peptide affinity reagents

Mirao Zha; Ping Lin; Hongwei Yao; Yibing Zhao; Chuanliu Wu

doi:10.1039/c7cc09142g

A phage display-based strategy for the de novo creation of disulfide-constrained and isomer-free bicyclic peptide affinity reagents

Chem Commun (Camb). 2018 Apr 17;54(32):4029-4032. doi: 10.1039/c7cc09142g.

Authors

Mirao Zha¹, Ping Lin, Hongwei Yao, Yibing Zhao, Chuanliu Wu

Affiliation

¹ Department of Chemistry, College of Chemistry and Chemical Engineering, The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, State Key Laboratory of Physical Chemistry of Solid Surfaces, Xiamen University, Xiamen, 361005, P. R. China. chlwu@xmu.edu.cn.

PMID: 29619474
DOI: 10.1039/c7cc09142g

Abstract

Bicyclic peptides have been attractive scaffolds for developing high affinity reagents for biomacromolecules. Here we report a general phage-screening strategy for the development of bicyclic peptide ligands constrained with isomerically-forbidden disulfide bridges without elaborate chemical modifications and recourses to genetic code reprogramming.

MeSH terms

Amino Acid Sequence
Bridged Bicyclo Compounds, Heterocyclic / chemical synthesis*
Bridged Bicyclo Compounds, Heterocyclic / chemistry
Cell Surface Display Techniques / methods*
Consensus Sequence
Cysteine / chemistry
Disulfides / chemical synthesis*
Disulfides / chemistry
Isomerism
Kelch-Like ECH-Associated Protein 1 / chemistry
Ligands
Oxidation-Reduction
Penicillamine / chemistry
Peptides, Cyclic / chemical synthesis*
Peptides, Cyclic / chemistry

Substances

Bridged Bicyclo Compounds, Heterocyclic
Disulfides
Kelch-Like ECH-Associated Protein 1
Ligands
Peptides, Cyclic
Penicillamine
Cysteine