Jump to main content
Jump to site search

Issue 12, 2012
Previous Article Next Article

Synthesis and binding affinities for sst receptors of cyclic peptoid SRIF-mimetics

Author affiliations

Abstract

Mimicking the tetradecapeptide somatostatin through the design of novel non-peptide small molecules is needed for developing analogues with selective or universal affinity for human somatostatin receptors (hsst1–5) and improved pharmacological properties. We report the synthesis and evaluation of the binding potential of the first all-peptoid SRIF (somatotropin release-inhibiting factor) analogues. Cyclic β and mixed α/β tetra- or pentapeptoids were efficiently obtained by macrocyclisation of the corresponding linear peptoids. In vitro competition binding experiments using [125I]-somatostatin were performed on this first generation of peptoids mimicking the SRIF pharmacophore (Phe7-(D)Trp8-Lys9-Thr10). The selectivity profiles of cyclic compounds 1 to 4 were similar with higher affinity for the sst3, sst5 and sst4 receptors and lower potency on sst1 and sst2 subtypes.

Graphical abstract: Synthesis and binding affinities for sst receptors of cyclic peptoid SRIF-mimetics

Back to tab navigation

Supplementary files

Publication details

The article was received on 06 Sep 2012, accepted on 09 Oct 2012 and first published on 09 Oct 2012


Article type: Concise Article
DOI: 10.1039/C2MD20265D
Citation: Med. Chem. Commun., 2012,3, 1531-1535
  •   Request permissions

    Synthesis and binding affinities for sst receptors of cyclic peptoid SRIF-mimetics

    C. Caumes, T. Hjelmgaard, O. Roy, M. Reynaud, D. Servent, C. Taillefumier and S. Faure, Med. Chem. Commun., 2012, 3, 1531
    DOI: 10.1039/C2MD20265D

Search articles by author

Spotlight

Advertisements