189131-85-9Relevant academic research and scientific papers
Carbachol dimers with primary carbamate groups as homobivalent modulators of muscarinic receptors
Bartz, Ulrike,Bellucci, Cristina,Dei, Silvia,Holze, Janine,Manetti, Dina,Martino, Maria Vittoria,Matucci, Rosanna,Mazzolari, Angelica,Mohr, Klaus,Nesi, Marta,Romanelli, Maria Novella,Teodori, Elisabetta,Tr?nkle, Christian,Vistoli, Giulio,Welzel, Jessica
, (2020)
Although agonists and antagonists of muscarinic receptors have been known for long time, there is renewed interest in compounds (such as allosteric or bitopic ligands, or biased agonists) able to differently and selectively modulate these receptors. As a continuation of our previous research, we designed a new series of dimers of the well-known cholinergic agonist carbachol. The new compounds were tested on the five cloned human muscarinic receptors (hM1–5) expressed in CHO cells by means of equilibrium binding experiments, showing a dependence of the binding affinity on the length and position of the linker connecting the two monomers. Kinetic binding studies revealed that some of the tested compounds were able to slow the rate of NMS dissociation, suggesting allosteric behavior, also supported by docking simulations. Assessment of ERK1/2 phosphorylation on hM1, hM2 and hM3 activation showed that the new compounds are endowed with muscarinic antagonist properties. At hM2 receptors, some compounds were able to stimulate GTPγS binding but not cAMP accumulation, suggesting a biased behavior. Classification, Molecular and cellular pharmacology.
Conformationally constrained [p-(ω-aminoalkyl)phenacetyl]-L-seryl-L- lysyl dipeptide amides as potent peptidomimetic inhibitors of Candida albicans and human myristoyl-CoA:protein N-myristoyl transferase
Nagarajan, Srinivasan R.,Devadas, Balekudru,Zupec, Mark E.,Freeman, Sandra K.,Brown, David L.,Lu, Hwang-Fun,Mehta, Pramod P.,Kishore, Nandini S.,McWherter, Charles A.,Getman, Daniel P.,Gordon, Jeffrey I.,Sikorski, James A.
, p. 1422 - 1438 (2007/10/03)
MyristoylCoA:protein N-myristoyltransferase (NMT) covalently attaches the 14-carbon saturated fatty acid myristate, via an amide bond, to the N- terminal glycine residues of a variety of cellular proteins. Genetic studies have shown that NMT is essential
