Bridged peptides including stapled peptides are attractive tools for regulating protein-protein interactions (PPIs). An effective synthetic methodology in a heterogeneous system for the preparation of these peptides using olefin metathesis and hydrogenation of protected peptides with a long aliphatic chain anchor is reported.

Spatiotemporal control of peptide nanofibre growth was achieved by photocleavage of a DNA-conjugated β-sheet forming peptide that is linked through a photoresponsive amino acid residue. Peptide nanofibres were selectively formed by photocleaving the conjugate on a complementary DNA-immobilised glass substrate.

Thioester-producing protocol featuring carboxypeptidase Y (CPaseY)-mediated hydrazinolysis and subsequent self-editing of tag affords protein thioesters in a traceless manner.

A traceable linker that is potentially applicable to identification of a target protein of bioactive compounds was developed. It enabled not only thiol-induced cleavage of the linker for enrichment of the target protein but also selective labelling to pick out the target from contaminated non-target proteins for facile identification.

Oxidative stress-responsive compounds are attracting significant attention in the field of medicinal chemistry and chemical biology. Here, we disclose the development of a hydrogen peroxide (H2O2)-responsive amino acid that induces peptide bond cleavage in the presence of H2O2 that closely relates to the oxidative stress. The H2O2-responsive amino acid possessing a boronate or boronic acid moiety was incorporated into a peptide using Fmoc-based solid-phase peptide synthesis or that with minor modification, respectively, and the peptide bond cleavage of the obtained peptide was successfully triggered by the addition of H2O2.