Journal article

Peptide folding induces high and selective affinity of a linear and small beta-peptide to the human somatostatin receptor 4

K Gademann, T Kimmerlin, D Hoyer, D Seebach

Journal of Medicinal Chemistry | AMER CHEMICAL SOC | Published : 2001

Abstract

beta-Peptides with side chains in the 2- and 3-positions on neighboring residues (of (S) configuration) are known to fold and form a turn (similar to an alpha-peptidic beta-turn). Thus, we have synthesized an appropriately substituted beta-tetrapeptide derivative to mimic the hormone somatostatin in its binding to the human receptors hsst(1-5), which is known to rest upon a turn containing the amino acid residues Thr, Lys, Trp, and Phe. The N-acetyl-peptide amide Ac-beta(3)-HThr-beta(2)-HLys-beta(3)-HTrp-beta(3)-HPhe-NH(2) (1) indeed shows all characteristics of the targeted turn-mimic: Lys CH(2) groups are in the shielding cone of the Trp indole ring (by NMR analysis, Figure 2) and there is..

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University of Melbourne Researchers