A convergent strategy for glycoprotein synthesis entails the assembly of individual peptidyl
substrates, each bearing a single carbohydrate domain. These subunits would then be …

Native chemical ligation (NCL) is an extremely useful technique for the synthesis of peptide
and protein targets.[1, 2] The method, which relies on the chemoselective condensation of a …

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 …

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 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 …

In recent years, there has been an explosion of interest in protein-assembly technologies
such as native chemical ligation (NCL)[1] and expressed protein ligation (EPL).[2] NCL …

Over half of all proteins in nature are estimated to be glycosylated,[1] and these
biomolecules play key roles in protein expression, folding and stability [2–7] and are …

The discovery of native chemical ligation (NCL) by Kent and co-workers in 1994 was a
critical step, enabling researchers to chemically access medium-sized proteins through total …

Protein glycosylation comprises a large family of posttranslational modifications in
eukaryotic organisms and is biosynthetically mediated by numerous glycosyltransferases.[1] …