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 …

Advances in the site-specific chemical modification of proteins, also referred to as protein
bioconjugation, have proved instrumental in revolutionary approaches to designing new …

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 …

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 …

Peptide and protein thioesters are playing an increasingly prominent role in the chemical
toolbox for protein assembly and modification through Native Chemical Ligation (NCL). In …

In 1998, the Ramage group demonstrated that a C-terminal hydrazide of a synthetic peptide
could, following diazotization to the corresponding acyl azide, be transformed into usefully …

The reversible post‐translational modification of eukaryotic proteins by ubiquitin regulates
key cellular processes including protein degradation and gene transcription. Studies of the …

N‐Sulfanylethylanilide (SEAlide) peptides were developed with the aim of achieving facile
synthesis of peptide thioesters by 9‐fluorenylmethyloxycarbonyl (Fmoc)‐based solid‐phase …

The method of native chemical ligation between an unprotected peptide α‐thioester and an
N‐terminal cysteine–peptide to give a native peptide in aqueous solution is one of the most …

The design and synthesis of biomolecules that are responsive to external stimuli is of great
interest in various research areas, such as in the preparation of smart biomaterial and …