All-hydrocarbon stapled peptides make up a promising class of protein–protein interaction
regulators; their potential therapeutic benefit arises because they have a high binding affinity …

Hydrocarbon-stapled α-helical peptides are a new class of targeting molecules capable of
penetrating cells and engaging intracellular targets formerly considered intractable. This …

Hydrocarbon-stapled peptides are a class of bioactive alpha-helical ligands developed to
dissect and target protein interactions. While there is consensus that stapled peptides can …

The stereochemical effects of the hydrocarbon crosslink on the conformation and cellular
uptake of i, i+ 4 stapled peptides were studied. Compared to its S, S-configurated …

Linear peptides can mimic and disrupt protein-protein interactions involved in critical cell
signaling pathways. Such peptides however are usually protease sensitive and unable to …

Stapled α-helical peptides represent an emerging superclass of macrocyclic molecules with
drug-like properties, including high-affinity target binding, protease resistance, and …

Purpose. To investigate the relationships between the β-turn structure of a peptide and its
passive diffusion across Caco-2 cell monolayers, an in vitro model of the intestinal mucosa …

Stapling of side chains to stabilize an α-helical structure has been generally associated with
an increased uptake of CPPs. Here, we compare four amphiphilic stapled peptides with their …

Most protein–protein interactions occur inside cells. Peptides can inhibit protein–protein
interactions but tend not to enter cells. We systematically compare cell permeability for 8–12 …

Stapled peptides have emerged as a new class of targeting molecules with high binding
affinity and specificity for intracellular undruggable targets. Their ability to penetrate cell …