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Peptide-oligourea hybrids analogue of GLP-1 with improved action in vivo

Author

Listed:
  • Juliette Fremaux

    (UREKA—ImmuPharma Group)

  • Claire Venin

    (UREKA—ImmuPharma Group)

  • Laura Mauran

    (UREKA—ImmuPharma Group)

  • Robert H. Zimmer

    (UREKA—ImmuPharma Group)

  • Gilles Guichard

    (Univ. Bordeaux, CNRS, CBMN, UMR 5248, Institut Européen de Chimie et Biologie)

  • Sébastien R. Goudreau

    (UREKA—ImmuPharma Group)

Abstract

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. 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. 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. 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. The efficacy of the approach is demonstrated with three GLP-1-oligourea hybrids showing prolonged activity in vivo. Our findings should enable the use of oligoureas in other peptides to improve their pharmaceutical properties and may provide new therapeutic applications.

Suggested Citation

  • Juliette Fremaux & Claire Venin & Laura Mauran & Robert H. Zimmer & Gilles Guichard & Sébastien R. Goudreau, 2019. "Peptide-oligourea hybrids analogue of GLP-1 with improved action in vivo," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08793-y
    DOI: 10.1038/s41467-019-08793-y
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