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

K Gademann, T Kimmerlin, D Hoyer…

Index: Gademann; Kimmerlin; Hoyer; Seebach Journal of Medicinal Chemistry, 2001 , vol. 44, # 15 p. 2460 - 2468

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Citation Number: 190

Abstract

β-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 α-peptidic β-turn). Thus, we have synthesized an appropriately substituted β-tetrapeptide derivative to mimic the hormone somatostatin in its binding to the human receptors hsst1-5, which is known to rest upon a turn containing the amino acid residues Thr, Lys, Trp, and Phe. The N-acetyl- ...