Herein, we describe the development and application of a novel expressed protein
selenoester ligation (EPSL) methodology for the one‐pot semi‐synthesis of modified …

Chemoselective peptide ligation methods have provided synthetic access to numerous
proteins, including those bearing native post-translational modifications and unnatural …

Employing selenocysteine-containing protein fragments to form the amide bond between
respective protein fragments significantly extends the current capabilities of the widely used …

Highlights•When selenoester is used for ligation reactions with diselenides, kinetics are
accelerated and side reactions are minimized.•Selenozolidine is emerging as the preferred …

The growing interest in proteins, both in fundamental research and in drug discovery, has
fuelled demand for efficient synthetic methods to access these biomolecules. Although solid …

We describe an unprecedented reaction between peptide selenoesters and peptide dimers
bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide …

Peptide selenoesters have recently emerged as key building blocks for the ligation-based
assembly of large polypeptides and proteins. Herein, we report an efficient solid-phase …

Mild strategies for the selective modification of peptides and proteins are in demand for
applications in therapeutic peptide and protein discovery, and in the study of fundamental …

Peptide ligation chemistry has revolutionized protein science by facilitating access to
synthetic proteins. Here, we describe the development of additive-free ligation …

Despite the unique chemical properties of selenocysteine (Sec), ligation at Sec is an under‐
utilized methodology for protein synthesis. We describe herein an unprecedented protocol …