Collect. Czech. Chem. Commun. 1994, 59, 2511-2522

Analogues of the Cholecystokinin C-Terminal Tetrapeptide

Jan Hlaváček, Renáta Marcová, Lenka Maletínská and Jiřina Slaninová

Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic


Substituted phenylethyl amides and phenylethyl esters Va - Vj derived from the carboxyterminal tetrapeptide part of the cholecystokinin were synthesized and their biological properties assayed. In the original CCK tetrapeptide structure Trp-Met-Asp-Phe-NH2 the Met was replaced by Lys(Pamc) and the terminal Phe-NH2 was replaced by Phe-NHCH2C6H5 or Phe-OCH2C6H5 moiety with a various degree of alkylation in the Ph ring. A bioassay revealed that these simple CCK analogues were selectively bound to A receptors from pancreas, whereas no binding to B receptors from brain was found. Some of the compounds behaved as weak inhibitors of CCK activity on gall bladder and guinea pig ileum contractions without any effect in anorectic assay.