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Issue 14, 2015
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Receptor-templated stapling of intrinsically disordered peptide ligands

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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

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Supplementary files

Article information


Submitted
06 Feb 2015
Accepted
02 Mar 2015
First published
02 Mar 2015

Org. Biomol. Chem., 2015,13, 4183-4189
Article type
Communication

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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