111540-45-5Relevant academic research and scientific papers
Synthesis and Biological Activity of CCK Heptapeptide Analogues. Effects of Conformational Constraints and Standard Modifications on Receptor Subtype Selectivity, Functional Activity in Vitro, and Appetite Suppression in Vivo
Holladay, Mark W.,Bennett, Michael J.,Tufano, Michael D.,Lin, C. W.,Asin, Karen E.,et al.
, p. 2919 - 2928 (2007/10/02)
A series of modifications of the CCK7 analogue (des-NH2)Tyr(SO3-)-Nle-Gly-Trp-Nle-Asp-Phe-NH2 was prepared and tested for binding to guinea pig CCK-A and CCK-B receptors and in CCK-A-mediated functional assays.Selected analogues also were teste
Development of Potent and Selective CCK-A Receptor Agonists from Boc-CCK-4: Tetrapeptides Containing Lys(Nε)-Amide Residues
Shiosaki, Kazumi,Lin, Chun Wel,Kopecka, Hana,Craig, Richard A.,Bianchi, Bruce R.,et al.
, p. 2007 - 2014 (2007/10/02)
A series of Boc-CCK-4 derivatives represented by the general structure Boc-Trp-Lys(Nε-COR)-Asp-Phe-NH2, where R is an aromatic, heterocyclic, or aliphatic group, are potent and selective CCK-A receptor agonists.These amide-bearing compounds complement the previously described urea-based tetrapeptides (Shiosaki et al.J.Med.Chem. 1991,34,2837-2842); structure-activity studies revealed parallel as well as divergent trends between these two series.A significant correlation was observed between pancreatic binding affinity and the resonance constant R of the phenyl substituent in one particular series of derivatives.Sulfation of phenolic amides appended onto the ε-amino group of the lysine did not affect affinity for the CCK-A receptor in contrast to the 500-fold increase in binding potency observed upon sulfation of CCK-8, suggesting that the lysine appendage and the sulfated tyrosine in CCK-8, both key structural elements that impart high affinity for the CCK-A receptor, are interacting differently with the receptor.The amide-bearing tetrapeptides are full agonists relative to CCK-8 in stimulating pancreatic amylase release while being partial agonists in eliciting phosphoinositide (PI) hydrolysis.Both effects were blocked by selective CCK-A receptor antagonists
