Of the many approaches proposed to generalize the native chemical ligation approach for
protein synthesis, the simple procedure of global desulfurization of peptide thiols has …

The native chemical ligation enables the chemoselective coupling of two unprotected
protein segments. In the initial format of this reaction, the side chain of N‐terminal cysteine …

The highly chemoselective reaction between unprotected peptides bearing an N-terminal
Cys residue and a C-terminal thioester enables the total and semi-synthesis of complex …

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 …

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

Disulfide bonds play an important role in both proteins and peptides. They cause
conformational constraints and increase the stability of such molecules. In nature, disulfide …

Cysteine‐based native chemical ligation (NCL) has been a very powerful approach for
convergent synthesis of peptides and proteins. However, owing to the low abundance of …

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 …

The combination of native chemical ligation and desulfurization is considered a powerful
strategy in protein synthesis. Homogeneous desulfurization conditions based on a radical …

The synthesis of proteins with a fully native sequence is an ongoing challenge in protein
chemistry. Native chemical ligation (NCL) approaches have proven to be generally …