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New approach set to make peptide stapling widely available

A team from the School of Chemistry has developed a new method for peptide stapling.

The approach is based on the reaction of two thiols in a peptide sequence with a dibromomaleimide reagent. When the two thiols are correctly placed in the peptide sequence the reaction results in the structure adopting a bioactive helical shape that is resistant to proteolytic degradation. The method works on peptide sequences containing the natural and common amino acids cysteine or homocysteine. This will permit access to stapled peptides via routine chemical and biological methods.

Professor Wilson, from the University of Leeds’ School of Chemistry and Astbury Centre for Structural Molecular Biology who led the team said: “Our approach to protein stapling is more flexible, potentially cheaper, and should be easier to use in chemical biology and drug discovery.

The full research paper Double Quick, Double Click Reversible Peptide ‘Stapling’ is published in the Royal Society of Chemistry’s Chemical Science journal.