Synthesis and in vitro characterization of new growth hormone secretagogues derived from ipamorelin with dipeptidomimetic N-terminals
作者:Bernd Peschke、Michael Ankersen、Birgit Sehested Hansen、Thomas Kruse Hansen、Nils Langeland Johansen、Jesper Lau、Kjeld Madsen、Hans Petersen、Henning Thøgersen、Brett Watson
DOI:10.1016/s0223-5234(99)80086-5
日期:1999.5
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. (C) Elsevier, Paris.