Journal article

New open-chain and cyclic tetrapeptides, consisting of alpha-, beta(2)-, and beta(3)-amino-acid residues, as somatostatin mimics - A survey

Dieter Seebach, Estelle Dubost, Raveendra I Mathad, Bernhard Jaun, Michael Limbach, Markus Loeweneck, Oliver Floegel, James Gardiner, Stefania Capone, Albert K Beck, Hans Widmer, Daniel Langenegger, Dominique Monna, Daniel Hoyer



Cyclo-β-tetrapeptides are known to adopt a conformation with an intramolecular transannular hydrogen bond in solution. Analysis of this structure reveals that incorporation of a β2-amino-acid residue should lead to mimics of 'α-peptidic β-turns' (cf. A, B, C). It is also known that short-chain mixed β/α-peptides with appropriate side chains can be used to mimic interactions between α-peptidic hairpin turns and G protein-coupled receptors. Based on these facts, we have now prepared a number of cyclic and open-chain tetrapeptides, 7-20, consisting of α-, β2-, and β3-amino-acid residues, which bear the side chains of Trp and Lys, and possess backbone configurations such that they should be capa..

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University of Melbourne Researchers