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Design and Synthesis of γ‐Dipeptide Derivatives with Submicromolar Affinities for Human Somatostatin Receptors
Author(s) -
Seebach Dieter,
Schaeffer Laurent,
Brenner Meinrad,
Hoyer Daniel
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200390205
Subject(s) - dipeptide , affinities , chemistry , stereochemistry , somatostatin , amide , peptide bond , receptor , peptide , binding affinities , side chain , combinatorial chemistry , biochemistry , biology , organic chemistry , endocrinology , polymer
A simple, designed, open‐chain γ‐dipeptide derivative (see picture; Nap=naphthyl), which contains only three amide bonds, can mimic the 14‐amino acid peptide hormone somatostatin. Surprisingly, the highest affinities ( K D ≈0.5 μ M ) for human receptors are observed when the “mandatory” Trp and Lys side chains on the turn mimic carry bulky substituents.