183483-09-2Relevant articles and documents
Synthesis and in vitro characterization of new growth hormone secretagogues derived from ipamorelin with dipeptidomimetic N-terminals
Peschke, Bernd,Ankersen, Michael,Sehested Hansen, Birgit,Kruse Hansen, Thomas,Langeland Johansen, Nils,Lau, Jesper,Madsen, Kjeld,Petersen, Hans,Thogersen, Henning,Watson, Brett
, p. 363 - 380 (2007/10/03)
The structural requirements for N-terminal features for the minimal structure of growth hormone secretagogues derived from ipamorelin are investigated. It is found, that incorporation of nonpolar peptidomimetic amino acids at the N-terminal can replace the Aib-His moiety and lead to compounds with high in vitro potency with respect to their growth hormone secretagogue properties. New unnatural amino acids with double bonds, ether- linkages, and 1,3-phenylene-moieties in the backbone proved to be valuable dipeptidomimetics. Using them, growth hormone secretagogues with high potencies were obtained.