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 substitution of primary or secondary alcohols with nucleophiles mediated by a redox
combination of a trialkylor triarylphosphine and a dialkyl azodicarboxylate is popularly …

Since the invention of solid phase synthetic methods by Merrifield in 1963, the number of
research groups focusing on peptide synthesis has grown exponentially. However, the …

Subtiligase-catalyzed peptide ligation is a powerful approach for site-specific protein
bioconjugation, synthesis and semisynthesis of proteins and peptides, and chemoproteomic …

Total chemical synthesis of proteins is usually achieved by assembling unprotected peptide
segments using site-specific and chemoselective native peptide ligation methods. Access to …

The reaction of a peptide featuring a bis (2-sulfanylethyl) amino (SEA) group on its C-
terminus with a cysteinyl peptide in water at pH 7 and 37° C leads to the chemoselective and …

The chemical synthesis of proteins provides synthetic chemists with an interesting challenge
and supports biological research through the generation of proteins that are not produced …

Peptide thioesters play a key role in convergent protein synthesis strategies such as native
chemical ligation, traceless Staudinger ligation, and Ag+‐mediated thioester ligation. The …

A new method for the preparation of peptide thioester by the post-solid phase peptide
synthesis (SPPS) approach was developed. A series of N-alkyl cysteine derivatives were …