Synthesis, conformational and biological properties of lipophilic derivatives of gastrin and cholecystokinin peptides
Abstrw: The fully active [Nle15]-little-gastrin-(2-17) and [Thr2s,Nle31]-CCK-(2533) were lipo-derivatized by N-terminal incorporation of di-fattyacyl-glycerol moieties. Although the induced tight interdigitation of the lipo-tail with the lipid compartments of cell membrane bilayers prevent an escape of the lipophilic hormones into the extracellular water phase, they retain high receptor binding affinities. This confirms that a membrane-bound pathway for hormone receptor recognition is possible, even if it implies lateral penetration of the complex channel type suprastructure by the ligand at the lipidlwater interface.