Indeed, peptides have proved to be valuable tools to access extra-cellular targets with medium to large active sites and they are now intensively investigated to access intracellular protein–protein interaction (PPI) targets, a very important topic in recent pharmaceutical research 5, 6, 7, 8, 9, 10. Our findings should enable the use of oligoureas in other peptides to improve their pharmaceutical properties and may provide new therapeutic applications.ĭuring the past decade, peptide therapeutics have gained considerable attention in pharmaceutical research and development (R&D) 1, 2, 3, 4. The efficacy of the approach is demonstrated with three GLP-1-oligourea hybrids showing prolonged activity in vivo. Our strategy consists in replacing four consecutive amino acids of GLP-1 by three consecutive ureido residues by capitalizing on the structural resemblance of oligourea and α-peptide helices. Here, we describe the use of oligourea foldamers as tool to improve the pharmaceutical properties of GLP-1, a 31 amino acid peptide hormone involved in metabolism and glycemic control. Despite substantial progress, the successful development of peptides as drugs still requires a number of limitations to be addressed, including short in vivo half-lives and poor membrane permeability. Peptides have gained so much attention in the last decade that they are now part of the main strategies, with small molecules and biologics, for developing new medicines.
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