Fluorescence studies on the binding between 1-47 fragment of cholecystokinin receptor CCKA-R(1-47) and nonsulfated cholecystokinin octapeptide CCK8

The interaction between the 1-47 N-terminus fragment of the cholecystokinin receptor and the nonsulfated cholecystokinin octapeptide, CCK8, is monitor ed by fluorescence emission. Quenching of the fluorescence intensities is o bserved on binding. Dissociation constants calculated by these data are in the same submicromolar range as found for the binding of linear CCK8 analog ues to B-type receptors. Although detailed structural information cannot be obtained, fluorescence emission is more sensitive than other techniques an d permits fast detection of receptor-ligand interaction. (C) 2001 John Wile y & Sons, Inc.