Synthesis, conformational and biological properties of lipophilic derivatives of gastrin and cholecystokinin peptides

Abstract

The fully active [Nle15]-little-gastrin-(2–17) and [Thr28,Nle31]-CCK-(25–33) 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 lipid/water interface. © 1994 IUPAC