Abstract
We report on the synthesis of some analogs of the C-terminal heptapeptide of cholecystokinin in which the C-terminal primary amide has been deleted and the L-tryptophan replaced by a D-tryptophan. These analogs were evaluated in vitro for their ability (i) to recognize the CCK receptor on rat pancreatic acini and on guinea pig brain membranes; (ii) to stimulate amylase release from rat pancreatic acini. Although previous works suggested that the C-terminal primary amide is essential for exhibiting a full biological response on pancreatic acini, this study does not confirm this hypothesis.
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