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Binding of Cholecystokinin‐8 (CCK‐8) Peptide Derivatives to CCK A and CCK B Receptors
Author(s) -
Schäfer Ute,
Harhammer Rainer,
Boomgaarden Monika,
Sohr Reinhard,
Ott Tilmann,
Henklein Peter,
Repke Heinrich
Publication year - 1994
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1994.62041426.x
Subject(s) - cholecystokinin , cholecystokinin receptor , receptor , pentapeptide repeat , norleucine , chemistry , peptide , radioligand , binding site , stereochemistry , biochemistry , amino acid , leucine
The structural requirements for the selective binding of cholecystokinin‐8 (CCK‐8)‐related peptides to peripheral (CCK A ) receptors are not sufficiently understood. In this study, the interaction of a series of newly shortened analogues of CCK‐8 with both receptor subtypes was analyzed by displacement studies using [ 3 H]‐CCK‐8 and 125 l‐Bolton‐Hunter (BH)‐CCK‐8 as radioligands. The pentapeptide derivative of CCK‐8, succinyl‐Tyr (SO 3 H)‐Met‐Gly‐Trp‐Met‐phenethylamide, was found to bind selectively with high affinity to the CCK A receptor. The replacement of Met 28 and/or Met 31 by norleucine and of L‐Trp 30 by its D‐analogue had no significant effect on the binding properties of the peptide. Further C‐terminal shortening resulted in a drastic loss of affinity and selectivity of the CCK receptor binding.