The facile rearrangement of “S-acyl isopeptides” to native peptide bonds via S, N-acyl shift is
central to the success of native chemical ligation, the widely used approach for protein total …

Highly chemoselective amide forming ligation reactions have facilitated the synthetic access
to proteins and other amide-linked bioconjugates. In order to generalize this approach, a Nα …

Intramolecular acyl transfer equilibrium in peptides and proteins has stimulated the
development of new methodologies for ligation, aggregation suppression or difficult peptide …

Protein chemical synthesis can overcome potential limitations of protein expression and
produce proteins with predesigned changes and modifications with atomic precision. The …

The amide linkage is generally considered to make amides the most stable carboxylic acid
derivatives, and this is one feature that contributes to their attractiveness as building blocks …

Highlights•Reversible covalent chemistry and peptide dynamic combinatorial libraries.•
Chemoselective reversible amide bond and peptide bond forming reactions.•Peptide …

The advent of kinetically controlled Native Chemical Ligation has permitted more efficient
sequential Native Chemical Ligation reactions to take place in one pot where one or more of …

O‐Acyl isopeptides, in which the N‐acyl linkage on the hydroxyamino acid residue (eg, Ser
and Thr) is replaced with an O‐acyl linkage, generally possess superior water‐solubility to …

Central to the understanding and use of peptides is the extent to which one can manipulate
the primary sequence. Complete control–through synthesis–of the primary sequence of a …

Chemoselective reactions for amide bond formation have transformed the ability to access
synthetic proteins and other bioconjugates through ligation of fragments. In these ligations …