The native chemical ligation reaction (NCL) involves reacting a C-terminal peptide thioester
with an N-terminal cysteinyl peptide to produce a native peptide bond between the two …

The present review offers an overview of nonclassical (eg, with no pre-or in situ activation of
a carboxylic acid partner) approaches for the construction of amide bonds. The review aims …

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 …

Protein semisynthesis—defined herein as the assembly of a protein from a combination of
synthetic and recombinant fragments—is a burgeoning field of chemical biology that has …

Cyclic peptides have been attracting a lot of attention in recent decades, especially in the
area of drug discovery, as more and more naturally occurring cyclic peptides with diverse …

Methods to prepare proteins that include a specific modification at a desired position are
essential for understanding their cellular functions and physical properties in living systems …

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

Selenocysteine, the selenium‐containing analogue of cysteine, is the twenty‐first
proteinogenic amino acid. Since its discovery almost fifty years ago, it has been exploited in …

The acetamidomethyl (Acm) moiety is a widely used cysteine protecting group for the
chemical synthesis and semisynthesis of peptide and proteins. However, its removal is not …

Sulfur and selenium occupy a distinguished position in biology owing to their redox
activities, high nucleophilicity, and acyl transfer capabilities. Thiolated/selenolated amino …