The rising demand for regioselective protein modifications in chemical biology and
pharmaceutical manufacturing has fueled efforts to develop diverse techniques that …

The properties of synthetic peptides, including potency, stability, and bioavailability, are
strongly influenced by modification of the peptide chain termini. Unfortunately, generally …

Site-specific protein modification techniques have led to breakthroughs across diverse
fields, such as cell imaging, proteomics, biomaterials, and pharmaceutical protein and …

The spatial alignment of functional groups is a central aspect of most catalytic processes.
Protein scaffolds with their exceptional molecular recognition properties have evolved into …

Directed peptides C-terminal modification enabled by the engineered biomolecular catalyst–
peptide amidase 12B has been achieved via computational protein engineering. The …

The escalating demand for biocatalysts in pharmaceutical and biochemical applications
underscores the critical imperative to enhance enzyme activity and durability under high …

Peptides are privileged ligands for diverse biomacromolecules, including proteins; however,
their utility is often limited due to low membrane permeability and in-cell instability. Here, we …

Chemical reactions can be performed to covalently modify specific residues in proteins.
When applied to native enzymes, these chemical modifications can greatly expand the …

Stapling has emerged as a powerful technique in peptide chemistry. It enables precise
control over peptide conformation leading to enhanced properties such as improved stability …

Highlights•Electrophiles can show distinct amino-acid selectivities in proteomes.•The
judicious selection of an electrophile is critical to various chemical-proteomic applications.•A …