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Cholecystokinin-octapeptide Fragments: Binding to Brain Cholecystokinin Receptors

Cholecystokinin-octapeptide Fragments: Binding to Brain Cholecystokinin Receptors

M Knight, C A Tamminga, L Steardo, M E Beck, P Barone, T N Chase

Eur J Pharmacol. 1984 Oct 1;105(1-2):49-55.

PMID: 6092115

Abstract:

Structural determinants of cholecystokinin octapeptide (CCK-8) binding to central nervous system receptors have been studied to assess the relative importance of the amino and the carboxyl end of the active peptide sequence, CCK-(26-33). The relative ability to inhibit equilibrium binding of [125I]CCK-33 to guinea pig cortical membranes was determined for a series of amino and carboxyl terminal fragments of CCK-8. While N-acetyl CCK-(26-29), N-acetyl CCK-(26-30) amide and N-acetyl CCK-(26-31) amide were inactive, the N-acetyl CCK-(26-32) amide fragment displayed binding to central receptors. Of the carboxyl terminal peptide fragments, both CCK-(29-33) and CCK-(30-33) bound less potently than CCK-8; CCK-(31-33) interacted more weakly than the tetra- and pentapeptide, but with a higher affinity to brain receptors than to peripheral receptors. The heptapeptide, CCK-(26-32) amide, and the tripeptide, CCK-(31-33), are known to antagonize CCK action at peripheral receptors. The heptapeptide bound to central receptors 25 times more potently than a known peripheral antagonist, dibutyryl cyclic GMP. Thus these peptides may act centrally to oppose CCK-8 mediated functions.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1947371	Cholecystokinin Fragment 30-33 Amide		1947-37-1	Price

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