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E Kostenis

Publications and source records attributed to E Kostenis.

24 records · Page 2Linked to original sources

Search for lead structures to develop new allosteric modulators of muscarinic receptors.

Various compounds are known to allosterically modulate the binding of ligands to muscarinic receptors. Most of these compounds have another predominant pharmacological action. Identification of the potent representatives should be useful for the development of allosteric modulators that are specific and highly active. For various reasons, a direct comparison of allosteric potencies on the basis of literature data is difficult. Therefore, a series of compounds was compared with regard to the allosteric delay of the dissociation of N-[3H]methylscopolamine from porcine heart M2 receptors under the following assay conditions: "Na,K,Pi buffer", 4 mM Na2HPO4, 1 mM KH2PO4, pH 7.4, 23 degrees C; "Mg,Tris,Cl,Pi buffer', 50 mM Tris-HCl, 3 mM MgHPO4,pH 7.3, 37 degrees C. Generally, the allosteric potency of the compounds was higher in the Na,K,Pi buffer, compared with the Mg,Tris,Cl,Pi buffer. However, the extent of the potency shift differed, ranging from approximately 2-fold for tacrine to approximately 100-fold for gallamine. The concentration retarding radioligand dissociation to half of the control rate (EC50) served as a measure of allosteric potency. Under both assay conditions, alcuronium was the most potent compound (EC50,Na,K,Pi = 4 nM and EC50,Mg,Tris,Cl,Pi = 55 nM), followed by alkane-bisammonium and bispyridinium compounds containing phthalimido moieties. Gallamine showed intermediate potency (EC50 values of 180 nM and 16,000 nM in Na,K,Pi buffer and Mg,Tris,Cl,Pi buffer, respectively). Obidoxime and hexamethonium, both known to antagonize allosteric actions, revealed submaximal efficacy and low potency (EC50,Na,K,Pi of approximately 100,000 nM). The relevance of these results, regarding the identification of lead structures for the development of new allosteric modulators, is discussed.

Alcuronium↗

Potentiation by alcuronium of the antimuscarinic effect of N-methylscopolamine in guinea pig left atria.

Alcuronium is known to stabilize allosterically the binding of the muscarinic antagonist N-methylscopolamine to muscarinic M2 receptors and thus to elevate the equilibrium binding of N-methylscopolamine in homogenized cardiac tissue. In order to check for a functional consequence of this effect, the action of alcuronium alone and in combination with N-methylscopolamine was determined in contracting guinea pig left auricles with oxotremorine-M as the negative inotropic agonist. For sake of comparison, the allosteric modulator W84 = hexane-1,6-bis(dimethyl-3'- phthalimidopropyl-ammonium bromide) was included. Alcuronium displayed a weak antimuscarinic action (pA2 = 5.7). In conjunction with 10(-7) M N-methylscopolamine, alcuronium (> or = 10(-6) M) induced a more pronounced antimuscarinic effect than expected for a combination of competitive antagonists. The extent of overadditivity with combinations of W84 and 10(-7) M N-methylscopolamine was smaller. In conclusion, alcuronium potentiates the antimuscarinic effect of N-methylscopolamine in contracting cardiac preparations with high effectivity.

Alcuronium↗

Variation of the oxime function of bispyridinium-type allosteric modulators of M2-cholinoceptors.

The bisbenzylether of the bispyridinium oxime, DUO 3-O (4,4'-Bis-[(2,6-dichlorobenzyloxyimino)-methyl]-1,1'-propane-1,3- diyl-bispyridinium dibromide), has been found to stabilize the antagonist binding to the M2-cholinoceptors which is indicative of an allosteric action. The oxygen of the oxime group was replaced with a nitrogen and a CH2-group leading to DUO 3-N and 3-C, respectively. The allosteric potency of the compounds was characterized by the concentrations which retarded the rate of dissociation of [3H]N-methyl-scopolamine from porcine cardiac cholinoceptors by a factor of 2 (EC50). The hydrazone derivative DUO 3-N was found to be the most active compound (ED50 = 2.7 microM) exceeding in activity DUO 3-O by a factor of 1.6 and DUO 3-C by a factor of 5. No correlation was found between the lipophilicity, determined as octanol/water partition coefficient, and the allosteric potency. The distribution of charges in the molecules was calculated by means of PEOE and displayed as Kohonen maps: The calculations exhibit a shift of the positive charge in the pyridinium ring from the nitrogen to the carbon atom in para-position when going from DUO 3-C to 3-O and 3-N. This shift parallels the rank order of the allosteric potency. From these results the conclusion has been drawn that the between distance the terminal ring-system and the positive charge is pivotal for the interaction of the allosteric modulators with the receptor protein.

Allosteric Regulation↗

[Omeprazole].

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Humans↗

Search for the pharmacophore of bispyridinium-type allosteric modulators of muscarinic receptors.

The bis(dichlorobenzyl) ether of the bispyridinium oxime TMB 4 stabilizes antagonist binding to M2-cholinoceptors which is indicative of an allosteric action. More than 10 derivatives of the lead compound were synthesized to investigate structure-activity relationships. The allosteric potency of the compounds was indicated by the concentrations which retarded the rate of dissociation of [3H]N-methylscopolamine from porcine cardiac cholinoceptors by a factor of 2 (EC50). Compared with TMB 4, the bis(dichlorobenzyl) derivative 4a displayed a more than 200-fold higher potency (EC50 = 4.7 microM). One of the dichlorobenzyl groups could be replaced by a methyl group without loss of activity (EC50 = 4.5 microM). Further shortening of this end of the molecule was accompanied by a moderate decline in potency to a minimum of EC50 = 26 microM. The second quaternary nitrogen was not a prerequisite for an allosteric activity. It is concluded that one half of the lead compound is pivotal for an interaction with the allosteric site of the M2-cholinoceptor, whereas the opposite end of the molecule modulates the allosteric activity.

Allosteric Regulation↗

Structure-function analysis of muscarinic acetylcholine receptors.

The structural basis underlying the G protein coupling selectivity of different muscarinic receptor subtypes was analyzed by using a combined molecular genetic/biochemical approach. These studies led to the identification of key residues on the receptors as well as the associated G proteins that are critically involved in determining proper receptor/G protein recognition. Mutational analysis of the m3 muscarinic receptor showed that most native cysteine residues are not required for productive receptor/G protein coupling. The putative extracellular disulfide bond was found to be essential for efficient trafficking of the receptor protein to the cell surface but not for receptor-mediated G protein activation.

Amino Acid Sequence↗