The development of constrained peptides for inhibition of protein–protein interactions is an
emerging strategy in chemical biology and drug discovery. This manuscript introduces a …

Macrocyclic peptides are highly promising as inhibitors of protein–protein interactions. While
many bond-forming reactions can be used to make cyclic peptides, most have limitations …

A large proportion of protein–protein interactions (PPIs) occur between a short peptide and a
globular protein domain; the peptides involved in surface interactions play important roles …

The development of constrained peptides represents an emerging strategy to generate
peptide based probes and hits for drug-discovery that address challenging protein–protein …

The sheer size and vast chemical space (ie, diverse repertoire and spatial distribution of
functional groups) underlie peptides' ability to engage in specific interactions with targets of …

Two polar hinges for cyclization of peptides have been developed, leading to bicyclic
peptides and cyclized peptides with improved solubility and biological activity. Increasingly …

Introduction: Protein-protein interactions are predominant in the workings of all cells. Until
now, there have been a few successes in targeting protein-protein interactions with small …

Highlights•One of the most widely adopted strategies for α-helix stabilisation is peptide
stapling.•Stapled peptides are highly promising therapeutic agents.•General design …

Given the ubiquity of the⍺‐helix in the proteome, there has been much research in
developing mimics of⍺‐helices, and most of this study has been toward developing protein …

Stapling has emerged as a powerful technique in peptide chemistry. It enables precise
control over peptide conformation leading to enhanced properties such as improved stability …