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Fluorescence studies on the binding between 1–47 fragment of cholecystokinin receptor CCK A ‐R(1–47) and nonsulfated cholecystokinin octapeptide CCK8
Author(s) -
Ragone Raffaele,
De Luca Stefania,
Tesauro Diego,
Pedone Carlo,
Morelli Giancarlo
Publication year - 2000
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)56:1<47::aid-bip1042>3.0.co;2-r
Subject(s) - chemistry , fluorescence , cholecystokinin , cholecystokinin receptor , receptor , dissociation (chemistry) , dissociation constant , quenching (fluorescence) , biophysics , binding site , stereochemistry , peptide , ligand (biochemistry) , biochemistry , organic chemistry , physics , quantum mechanics , biology
The interaction between the 1–47 N‐terminus fragment of the cholecystokinin receptor and the nonsulfated cholecystokinin octapeptide, CCK8, is monitored by fluorescence emission. Quenching of the fluorescence intensities is observed on binding. Dissociation constants calculated by these data are in the same submicromolar range as found for the binding of linear CCK8 analogues to B‐type receptors. Although detailed structural information cannot be obtained, fluorescence emission is more sensitive than other techniques and permits fast detection of receptor–ligand interaction. © 2001 John Wiley & Sons, Inc. Biopolymers 56: 47–53, 2001