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 synthesis of proteins by native chemical ligation greatly enhances the application of
chemistry to complex molecules such as proteins. The essential building blocks for this …

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 …

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

Given the potential of peptide selenoesters for protein total synthesis and the paucity of
methods for the synthesis of these sensitive peptide derivatives, we sought to explore the …

The synthesis of suitably protected β-selenophenylalanine and β-selenoleucine amino acids
was accomplished from Garner's aldehyde as a common starting point. These selenoamino …

An efficient synthetic route to a suitably protected β-selenol-phenylalanine derivative from
commercially available Garner's aldehyde is described. The incorporation of this building …

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