Binding of Cholecystokinin-8 (CCK-8) Peptide Derivatives to CCKA and CCKB Receptors
| Autor: | Heinrich Repke, Monika Boomgaarden, Reinhard Sohr, Rainer Harhammer, Ute Schäfer, Tilmann Ott, Peter Henklein |
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| Rok vydání: | 2008 |
| Předmět: |
Male
Molecular Sequence Data Norleucine Succinimides Peptide Biology Binding Competitive digestive system Biochemistry Cholecystokinin receptor Pentapeptide repeat Sincalide Structure-Activity Relationship Cellular and Molecular Neuroscience chemistry.chemical_compound Animals Structure–activity relationship Amino Acid Sequence Rats Wistar Receptor Peptide sequence Cholecystokinin chemistry.chemical_classification digestive oral and skin physiology Peptide Fragments Rats Kinetics chemistry Indicators and Reagents Receptors Cholecystokinin hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of Neurochemistry. 62:1426-1431 |
| ISSN: | 0022-3042 |
| DOI: | 10.1046/j.1471-4159.1994.62041426.x |
| Popis: | The structural requirements for the selective binding of cholecystokinin-8 (CCK-8)-related peptides to peripheral (CCKA) 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 [3H]-CCK-8 and 125I-Bolton-Hunter (BH)-CCK-8 as radioligands. The pentapeptide derivative of CCK-8, succinyl-Tyr (SO3H)-Met-Gly-Trp-Met-phenethylamide, was found to bind selectively with high affinity to the CCKA receptor. The replacement of Met28 and/or Met31 by norleucine and of L-Trp30 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. |
| Databáze: | OpenAIRE |
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