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 …

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

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

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

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

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

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 …

Main observation and conclusion Selenoesters are useful substitutes for traditional
thioesters in protein ligation chemistry due to their high reactivity in the trans‐thio …

The convergent assembly of peptide fragments by native chemical ligation has
revolutionized the way in which proteins can be accessed by chemical synthesis. A variation …

The development of site‐selective chemistry targeting the canonical amino acids enables
the controlled installation of desired functionalities into native peptides and proteins. Such …