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.