Issue 14, 2015

Receptor-templated stapling of intrinsically disordered peptide ligands

Abstract

We report here a chemoselective peptide “stapling” method that can be performed on ligand–receptor complexes in situ. An appropriately structured macrocyclic bis-oxime linkage is shown to improve the affinity of a peptide ligand for its native protein receptor. The presence of the receptor as a template to preorganize the ligand into its bioactive conformation is found to bias reaction outcomes, suggesting the potential application of the method for receptor-assisted selection of stapled peptides.

Graphical abstract: Receptor-templated stapling of intrinsically disordered peptide ligands

Supplementary files

Article information

Article type
Communication
Submitted
06 Feb 2015
Accepted
02 Mar 2015
First published
02 Mar 2015

Org. Biomol. Chem., 2015,13, 4183-4189

Receptor-templated stapling of intrinsically disordered peptide ligands

C. M. Haney and W. S. Horne, Org. Biomol. Chem., 2015, 13, 4183 DOI: 10.1039/C5OB00269A

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