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Related Experiment Video

Updated: Jun 19, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Bioinspired peptide stapling generates stable enzyme inhibitors.

Richard Morewood¹, Christoph Nitsche¹

¹Research School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia. christoph.nitsche@anu.edu.au.

Chemical Communications (Cambridge, England)

|September 7, 2022

Summary

Researchers developed a novel peptide stapling method using a lanthionine ketenamine mimic. This technique enhances peptide drug candidates, leading to potent Zika virus protease inhibitors with improved enzyme inhibition.

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Published on: September 28, 2022

Area of Science:

Medicinal Chemistry
Organic Synthesis
Virology

Background:

Peptide stapling enhances the drug-like properties of peptides, improving their stability and bioavailability.
Natural metabolites like lanthionine ketenamine offer inspiration for novel chemical strategies.
Developing effective inhibitors against viral proteases is crucial for antiviral drug discovery.

Purpose of the Study:

To introduce a new peptide stapling strategy inspired by lanthionine ketenamine.
To demonstrate the utility of this method in developing cyclic peptide inhibitors of the Zika virus protease.
To investigate the impact of linker length on the activity of stapled peptide inhibitors.

Main Methods:

A novel peptide stapling reaction was developed, proceeding in aqueous conditions and orthogonal to standard amino acid chemistry.
The strategy allows for the incorporation of tailored linkers between peptide residues.
The method was applied to synthesize cyclic peptide inhibitors targeting the Zika virus protease.

Main Results:

The new peptide stapling strategy was successfully implemented.
The length of the peptide staple linker was identified as a critical factor for optimizing inhibitory activity.
The most effective stapled peptide inhibitor exhibited a tenfold increase in enzyme inhibition compared to its linear counterpart.

Conclusions:

The developed lanthionine ketenamine-mimicking peptide staple provides a versatile and efficient method for creating enhanced peptide drug candidates.
This approach is valuable for discovering potent inhibitors of viral proteases, such as the Zika virus protease.
Optimizing linker length in stapled peptides is essential for maximizing therapeutic efficacy.