C-Terminal residues play a pivotal role in dictating the structure and functions of proteins.
Herein, we report a mild, efficient, chemoselective, and site-selective chemical method that …

The properties of synthetic peptides, including potency, stability, and bioavailability, are
strongly influenced by modification of the peptide chain termini. Unfortunately, generally …

We hypothesize that substitution of α‐amino acids at or around the scissile bond of a peptide
substrate with β‐amino acids (containing an extra carbon in the peptide backbone) will …

A key goal of synthetic biology is to enable designed modification of peptides and proteins,
both in vivo and in vitro. N-and C-Terminal modification enzymes are crucial in this regard …

The X-ray crystal structure of the complex of carboxypeptidase A (CPA) and Gly-Tyr, has
been documented. The crystal structure reveals that both the amide carbonyl oxygen and …

Peptides respresent intriguing materials to achieve sustainable catalytic reactivity that mimic
the natural functions of enzymes, but without the limitations of temperature/solvent …

Chemoenzymatic peptide synthesis is potentially the most cost‐efficient technology for the
synthesis of short and medium‐sized peptides with some important advantages. For …

Chemoenzymatic protein and peptide modification is a powerful means of generating
defined, homogeneous conjugates for a range of applications. However, the use of …

Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical
modification that provides invaluable information regarding protein sequence, and it acts as …

We reported recently a new strategy for inactivation of carboxypeptidase A (CPA), a
prototypic metalloprotease, which exploited the active site zinc ion in its irreversible …