Collection of Czechoslovak Chemical Communications - digital archive 

Abstract

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.