In recent decades, peptides as potential drugs were more and more explored with the
development of non-oral medicine. There into, sulfur-containing peptide is one of the most …

The article presents a study of chemoselective peptide ligation-desulfurization to a protected
β-mercapto aspartate (Asp) residue. It develops an scalable route to a protected β-mercapto …

Protein action in nature is generally controlled by the amount of protein produced and by
chemical modification of the protein, and both are often perturbed in cancer. The amino acid …

Disulfide bonds (SS bonds) are important post-translational modifications of proteins. They
stabilize a three-dimensional (3D) structure (structural SS bonds) and also have the catalytic …

Highlights•Recent progress in ligation chemistry for the synthesis of peptides and proteins is
outlined.•Extensions of native chemical ligation at thiol and selenol amino acids.•New C …

Tyrosine sulfation is one of the most common post‐translational modifications in secreted
and transmembrane proteins and a key modulator of extracellular protein‐protein …

Introduction Sulfur-containing functional groups are privileged motifs that occur in various
pharmacologically effective substances and several natural products. Various functionalities …

Despite six decades of efforts to synthesize peptides and proteins bearing multiple disulfide
bonds, this synthetic challenge remains an unsolved problem in most targets (eg, knotted …

Tris (2-carboxyethyl) phosphine (TCEP) is a widely used substitute for dithiothreitol (DTT) in
the reduction of disulfide bonds in biochemical systems. Although TCEP has been recently …

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