Peptide and protein selective modification at tyrosine residues has become an exploding
field of research as tyrosine constitutes a robust alternative to lysine and cysteine-targeted …

Peptides are increasingly important drug candidates, offering numerous advantages over
conventional small molecules. However, they face significant challenges related to stability …

The ability of alkylamines to spontaneously liberate hydride ions is typically restrained,
except under specific intramolecular reaction settings. Herein, we demonstrate that this …

Peptide modification methods that do not rely on the cysteine residue are underdeveloped,
and their development could greatly expand the current toolbox for peptide chemistry …

There is a growing interest in constructing multicyclic peptide structures to expand the
chemical space of peptides. Conventional strategies for constructing large peptide structures …

Amino groups are common in both natural and synthetic compounds and offer a very
attractive class of endogenous handles for bioconjugation. However, the ability to …

Bicyclic peptides have emerged as one of the driving forces within the constrained peptide
family. Due to their unique pharmaceutical attributes, peptide bicycles have garnered a …

Abstract α‐Ketoaldehydes play versatile roles in the ubiquitous natural processes of protein
glycation. However, leveraging the reactivity of α‐ketoaldehydes for biomedical applications …

We report a minimalist gaseous sulfonyl-chloride-derived reagent for multicomponent
bioconjugation with amine, phenol, or aniline reagents to afford urea or carbamate products …

A tyrosine (Tyr)‐or tryptophan (Trp)‐selective metal‐free C− H sulfenylation reaction using
an acid‐activated S‐acetamidomethyl cysteine (Cys) sulfoxide, Cys (Acm)(O), has been …