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 …

Today, Fmoc SPPS is the method of choice for peptide synthesis. Very‐high‐quality Fmoc
building blocks are available at low cost because of the economies of scale arising from …

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 …

Intramolecular ligation of peptide hydrazides is reported to occur readily, causing the
lactamization of fully unprotected peptides in an epimerization-free manner. This method …

Controlling the topology of polymer-modified proteins has attracted growing interest.
However, one of the main challenges in this field is the lack of efficient and site-specific …

With two β-mercaptoethyl groups on the N, a tertiary amide of structure 1 is always poised for
intramolecular thioesterification however it flips about the C− N bond. It is shown that a …

An operationally simple method for the synthesis of peptide thioesters is developed using
standard Fmoc solid-phase peptide synthesis procedures. The method relies on the use of a …

G protein-coupled receptors (GPCRs) represent important drug targets, as they regulate
pivotal physiological processes and they have proved to be readily druggable. Natural …

The chemical synthesis of peptides or small proteins is often an important step in many
research projects and has stimulated the development of numerous chemical …