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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↗

A family of highly selective allosteric modulators of the metabotropic glutamate receptor subtype 5.

We have identified a family of highly selective allosteric modulators of the group I metabotropic glutamate receptor subtype 5 (mGluR5). This family of closely related analogs exerts a spectrum of effects, ranging from positive to negative allosteric modulation, and includes compounds that do not themselves modulate mGluR5 agonist activity but rather prevent other family members from exerting their modulatory effects. 3,3'-Difluorobenzaldazine (DFB) has no agonist activity, but it acts as a selective positive allosteric modulator of human and rat mGluR5. DFB potentiates threshold responses to glutamate, quisqualate, and 3,5-dihydroxyphenylglycine in fluorometric Ca2+ assays 3- to 6-fold, with EC50 values in the 2 to 5 microM range, and at 10 to 100 microM, it shifts mGluR5 agonist concentration-response curves approximately 2-fold to the left. The analog 3,3'-dimethoxybenzaldazine (DMeOB) acts as a negative modulator of mGluR5 agonist activity, with an IC50 of 3 microM in fluorometric Ca2+ assays, whereas the analog 3,3'-dichlorobenzaldazine (DCB) does not exert any apparent modulatory effect on mGluR5 activity. However, DCB seems to act as an allosteric ligand with neutral cooperativity, preventing the positive allosteric modulation of mGluRs by DFB as well as the negative modulatory effect of DMeOB. None of these analogs affects binding of [3H]quisqualate to the orthosteric (glutamate) site, but they do inhibit [3H]3-methoxy-5-(2-pyridinylethynyl)pyridine binding to the site for 2-methyl-6-(phenylethynyl)-pyridine, a previously identified negative allosteric modulator. With the use of these compounds, we provide evidence that allosteric sites on GPCRs can respond to closely related ligands with a range of pharmacological activities from positive to negative modulation as well as to neutral competition of this modulation.

Allosteric Regulation↗

Muscarinic allosteric modulators: atypical structure-activity-relationships in bispyridinium-type compounds.

Allosteric modulators of receptor binding are known for a variety of membrane receptors. In case of muscarinic receptors, a considerable number of structurally divergent modulators have been described. For the M2 receptor subtype which has a high sensitivity to allosteric modulation most of the allosteric agents bind to the common allosteric binding site of the receptor protein. In this study, a series of DUO compounds characterized by a bispyridinium middle chain and lateral benzyloximeether moieties of a systematically varied substitution pattern has been evaluated with regard to their allosteric potency to affect M2 receptors, whose orthosteric site was blocked by [3H]N-methylscopolamine. The variations in potency were found to be surprisingly small and the structure-activity relationships of the DUO compounds diverged from those of correspondingly substituted hexamethonio-type allosteric modulators. One has to conclude that DUO compounds bind in an "atypical" manner which is in agreement with recently reported side-directed mutagenesis and molecular modeling studies.

Allosteric Regulation↗

Allosteric modulators of G-protein-coupled receptors.

Allosteric modulators of G-protein-coupled receptors (GPCRs) interact with binding sites on the receptor that are topographically distinct from the orthosteric site recognized by the receptor's endogenous agonist. Allosteric modulators offer several advantages over standard orthosteric drugs, including the potential for greater receptor subtype selectivity. To date, the current paucity of clinically available allosteric drugs reflects the bias of traditional radioligand binding assays towards the detection of orthosteric effects. However, the advent of new cell-based high-throughput functional assays has led to an increased detection of allosteric GPCR ligands. The current challenge for modulator-based GPCR drug discovery is the optimization of both binding and functional assays to better detect and validate allosteric ligands.

Allosteric Regulation↗

Modeling the functional effects of allosteric modulators at pharmacological receptors: an extension of the two-state model of receptor activation.

Allosteric modulation is a mechanism for modifying pharmacological receptor activity that has largely been ignored in terms of therapeutic drug design, although benzodiazepine receptor ligands are an example of the serendipitous discovery of this class of compound. The current mathematical models of allosteric interactions at (particularly G-protein-coupled) receptors concentrate on the effects of the allosteric ligand on orthosteric ligand binding and ignore potential effects of these compounds on the ability of orthosteric ligands to cause receptor activation. In this report a mathematical model of allosteric interactions at pharmacological receptors has been investigated that explicitly includes effects of the allosteric ligand on receptor activation. This model uses the two-state model of receptor activation as its basis and is qualitatively consistent with currently reported behavior of allosteric modulators. The predictions of this model suggest a series of criteria that should be tested before the effects of an allosteric modulator can be quantified in a nonsystem-dependent manner. It has also been used to provide a potential mechanistic explanation for the functional effects of the A(1) adenosine receptor allosteric enhancer PD 81,723 and a recently reported allosteric modulator of type 1 metabotropic glutamate receptors.

Allosteric Regulation↗

Glutamate-based therapeutic approaches: allosteric modulators of metabotropic glutamate receptors.

Metabotropic glutamate receptors (mGluRs) have been proposed as novel targets for the treatment of a variety of disorders. Recently, highly selective allosteric modulators of the mGluRs have been developed by several groups. These allosteric compounds provide an unprecedented degree of selectivity for individual mGluRs, allowing for more detailed functional studies on the roles of these receptors. Furthermore, the allosteric approach avoids many of the hurdles associated with the development of direct agonists as drugs, and provides a clear path forward for clinical proof-of-concept studies. Currently, both positive allosteric modulators of mGluR2 and negative allosteric modulators of mGluR5 hold promise as novel anxiolytics, and positive allosteric modulators of mGluR4 appear to be an exciting new target for the treatment of Parkinson's disease.

Animals↗

[3H]N-methylscopolamine dissociation from muscarine receptors affected by low concentrations of allosteric modulators.

The ability of allosteric ligands to modulate the dissociation rate of [3H]N-methylscopolamine from atrial muscarinic receptors in the presence of varying concentrations of unlabelled N-methylscopolamine or atropine was evaluated. Gallamine, at a concentration approximating its KD value, slowed the dissociation of [3H]N-methylscopolamine in the presence of ca. 30 x KD of both unlabelled NMS or atropine. This was less evident when concentrations of ca. 1000 x KD of the unlabelled antagonists were employed. Similar findings were made with another allosteric modulator. These results indicate that gallamine can act allosterically at low concentrations.

Allosteric Regulation↗

Allosteric modulators and selective agonists of muscarinic receptors.

Allosteric modulators of ligand-receptor interactions are found for a variety of receptors (Christopoulos, 2002). Allosteric agents attach to a binding site being topographically distinct from the site for conventional (orthosteric) agonists or antagonists. In the case of the muscarinic receptor, a huge selection of structurally divergent modulators has been described for different receptor subtypes (Mohr et al., 2003). Alkane-bisammonio-type compounds carrying lateral phthalimido substituents are known to have a high affinity for the common allosteric binding site of the muscarinic acetylcholine M2 receptor (mAChR M2), which is already occupied by the orthosteric antagonist N-methylscopolamine (NMS). The resulting allosteric inhibition of the dissociation of [3H]NMS from the M2 receptors in porcine cardiac homogenates served to indicate binding of the test compounds to the allosteric site. Additionally, allosteric modulators can strongly influence equilibrium binding of the orthosteric ligand: Its binding can be reduced, left unaltered or elevated, and encoded as negative, neutral, and positive cooperativity, respectively (Christopoulos and Kenakin, 2002). The cooperativity is strongly dependent on the pair of allosteric/orthosteric ligands and on the receptor subtype.

Allosteric Regulation↗

Imidazenil, a partial positive allosteric modulator of GABAA receptors, exhibits low tolerance and dependence liabilities in the rat.

Long-term treatment of rats with full (triazolam) or selective (diazepam) allosteric modulators of gamma-aminobutyric acid type A (GABAA) receptors rapidly induced tolerance to the protective effect of these drugs against bicuculline-induced convulsion. In contrast, long-term administration of partial allosteric modulators (imidazenil and bretazenil) of GABAA receptors, in doses equipotent to those of diazepam and triazolam that induce anticonvulsant tolerance, failed to elicit such a tolerance. Furthermore, no cross-tolerance was observed between diazepam and imidazenil. Discontinuation of long-term treatment with diazepam or triazolam, but not of long-term treatment with imidazenil or bretazenil, sensitized rats to behavioral inhibition by punishment (electric shock) in a manner that was potentiated by flumazenil. Administration of a single oral dose of [14C]diazepam or [3H] imidazenil to rats treated repeatedly with the corresponding unlabeled drug or vehicle revealed that the brain concentrations of drugs and their metabolites were similar in both groups of animals. This suggests that tolerance to the full or selective allosteric modulators of GABAA receptors may be associated with changes in the efficacy of the allosteric modulation rather than with changes in drug metabolism. Imidazenil has a longer half-life than an equipotent dose of diazepam and protects rats against bicuculline-induced convulsions for a significantly longer time than diazepam or bretazenil.(ABSTRACT TRUNCATED AT 250 WORDS)

Allosteric Regulation↗

Identification of essential residues involved in the allosteric modulation of the human A(3) adenosine receptor.

We examined the effects on allosteric modulation and ligand binding of the mutation of amino acid residues of the human A(3) adenosine receptor (A(3)AR) that are hypothesized to be near one of three loci: the putative sodium binding site, the putative ligand binding site, and the DRY motif in transmembrane helical domain 3. The effects of three heterocyclic allosteric modulators [the imidazoquinoline 2-cyclopentyl-4-phenylamino-1H-imidazo[4,5-c]quinoline (DU124183), the pyridinylisoquinoline 4-methoxy-N-[7-methyl-3-(2-pyridinyl)-1-isoquinolinyl]benzamide (VUF5455), and the amiloride analog 5-(N,N-hexamethylene)-amiloride] on the dissociation of the agonist radioligand, N(6)- (4-amino-3-[(125)I]iodobenzyl)-5'-N-methylcarboxamidoadenosine, were compared at wild-type (WT) and mutant A(3)ARs. The F182A(5.43) and N274A(7.45) mutations eliminated the allosteric effects of all three modulators but had little effect on agonist binding. The N30A(1.50) and D58N(2.50) mutations abolished the allosteric effects of DU124183 and VUF5455, but not HMA, whereas the D107N(3.49) mutation abolished the effects of DU124183, but not HMA or VUF5455. The T94A(3.36), H95A(3.37), K152A(EL2), W243A(6.48), L244A(6.49), and S247A(6.52) mutations did not influence allosteric effects of the modulators. Sodium ions (100 mM), which modulate agonist binding at a variety of receptors, caused an approximately 80% inhibition of agonist binding in WT A(3)ARs but did not show any effect on D58N(2.50), D107N(3.49), and F182A(5.43) mutant receptors. In contrast, NaCl induced a modest increase of agonist binding in N30A(1.50) and N274A(7.45) mutant receptors. NaCl decreased the dissociation rate of the antagonist radioligand [(3)H]8-ethyl-4-methyl-2-phenyl-(8R)-4,5,7,8-tetrahydro-1H-imidazo[2.1-i]purin-5-one (PSB-11) at the WT A(3)ARs, but not the D58N(2.50) mutant receptor. The results were interpreted using a rhodopsin-based molecular model of the A(3)AR to suggest multiple binding modes of the allosteric modulators.

Adenosine↗

Discovery of positive allosteric modulators of metabotropic glutamate receptor subtype 5 (mGluR5).

This review provides an overview of the drug discovery process used to identify, develop and characterize the first positive allosteric modulators of the metabotropic glutamate receptor (mGluR) subtype 5 (mGluR5). Discovery and optimization of three series of positive allosteric modulators are described, each using different approaches. The symmetric benzaldazine series was discovered and optimized from samples already existing in our sample collection without an active synthetic program to further elucidate SAR. This series yielded a family of highly selective pharmacological tools that produced positive, negative and neutral allosteric modulation of mGluR5 activity. The original compound in the benzamide series was discovered from screening and this series was optimized using an iterative library synthesis approach to explore SAR in each of three regions of the molecule. This series produced more potent positive allosteric mGluR5 modulators than the benzaldazine series which could be evaluated for their effect on mGluR5 in brain slice electrophysiological studies. The pyrazole series used a fragment library approach based on small structural motives from the benzamide series to discover lead compounds and establish SAR. This series produced still more potent positive allosteric mGluR5 modulators with improved pharmacokinetic and physical properties. These modulators showed efficacy in animal behavioral models in which other antipsychotic drugs were active. Evaluation of assay data in mathematical models of allosterism to constrain possible mechanisms of action is briefly discussed. Other reviews of this emerging field with different emphases have been published recently [1-3].

Allosteric Regulation↗

Application of a kinetic model to the apparently complex behavior of negative and positive allosteric modulators of muscarinic acetylcholine receptors.

The binding of allosteric modulators to G protein-coupled receptors (GPCRs) is often described by an equilibrium allosteric ternary complex model (ATCM). This study evaluated the effects of three modulators on the binding of [(3)H]N-methylscopolamine ([(3)H]NMS) to the human M(2) muscarinic acetylcholine receptor (mAChR). The binding of each modulator was more complex than predicted by the ATCM; the inhibitors heptane-1,7-bis-(dimethyl-3-phthalimidopropyl)-ammonium bromide and gallamine yielded biphasic curves that were described empirically by a two-site binding model, whereas the enhancer alcuronium yielded a bell-shaped curve. Radioligand dissociation assays revealed that the modulators retarded [(3)H]NMS kinetics such that the system never attained equilibrium. Subsequent application of a kinetic ATCM accommodated and quantified all experimental observations. Our findings confirm and extend previous studies on the use of a kinetic ATCM for mAChR allosteric enhancers, but also highlight how complex curves displayed by allosteric inhibitors can be misinterpreted in terms of multisite orthosteric binding. It is possible that similar behavior of other allosteric modulators at GPCRs may reflect nonequilibrium binding artifacts rather than deviation from an ATCM.

Allosteric Regulation↗

Effects of negative allosteric modulators of gamma-aminobutyric acidA receptors on complex behavioral processes in monkeys.

A multiple schedule of repeated acquisition and performance of conditional discriminations was used to characterize the effects of two negative allosteric modulators of the gamma-aminobutyric acid (GABAA) receptor (ethyl beta-carboline-3-carboxylate [beta-CCE] and N-methyl-beta-carboline-3-carboxamide [FG-7142]), a hallucinogenic beta-carboline derivative (harmine), a benzodiazepine receptor antagonist (flumazenil) and a positive allosteric modulator (alprazolam). In the acquisition component, subjects acquired a different discrimination each session. Acquisition of a discrimination was defined by a decrease in errors as the session progressed. In the performance component, the discrimination was the same each session. Responding in both components was maintained by food presentation under a variable-ratio schedule. Incorrect responses in both components produced a 5-sec timeout. Alprazolam (0.1-18 mg/kg), beta-CCE (0.01-0.32 mg/kg), FG-7142 (0.1-18 mg/kg) and harmine (0.1-1.8 mg/kg) all dose-dependently decreased response rate in both components. However, accuracy of responding-was differentially affected by the drugs. Alprazolam selectively and dose-dependently increased percent errors in acquisition, whereas beta-CCE increased acquisition errors only at the highest doses tested in each subject. In contrast, FG-7142 and harmine had no effects on percent errors at doses that virtually eliminated responding. In all cases, performance accuracy was generally not affected. Flumazenil, at doses that had little or no effect (0.1 and 0.32 mg/kg) or occasionally decreased response rates (1 mg/kg) when administered alone, dose-dependently antagonized the rate-decreasing and error-increasing effects of beta-CCE, FG-7142 and alprazolam. In contrast, flumazenil failed to antagonize the effects of harmine. Thus, the negative allosteric modulators only moderately disrupted acquisition in comparison with the positive allosteric modulator, but the effects of both types of modulator were antagonized by the benzodiazepine antagonist flumazenil.

Allosteric Regulation↗

Substituted pyrazinones, a new class of allosteric modulators for gamma-aminobutyric acidA receptors.

We discovered substituted pyrazinones as a new class of allosteric modulators of gamma-aminobutyric acid (GABA)A receptors. Prototype pyrazinones, U-92813 [1-(furfuryl)-3,5-dichloro-6-phenylpyrazinone] and U-94863 [1-benzyl-3,5-dichloro-6-(2-chlorophenyl)pyrazinone], potentiated GABA-mediated Cl- currents in cloned GABAA receptors with certain subtype selectivity. The drugs markedly enhanced the GABA response in the alpha 1 beta 2 gamma 2 and alpha 1 beta 2 subtypes but not in the alpha 1 gamma 2 and beta 2 gamma 2 subtypes expressed in human kidney cells. The dose-response profile of U-94863 in the alpha 1 beta 2 subtype was largely indistinguishable from that in the alpha 1 beta 2 gamma 2 subtype, suggesting no critical role for the gamma 2 subunit in potentiation of the GABA response by the pyrazinones. The drugs also potentiated the GABA response in the alpha 3 beta 2 gamma 2 and alpha 6 beta 2 gamma 2 subtypes, indicating their nonselectivity toward the alpha isotypes. With respect to subtype selectivity, the pyrazinones differ not only from ligands for benzodiazepine receptors, which interact only with the subtypes containing alpha beta gamma subunits, but also from barbiturates and neurosteroids, which interact with all the subtypes tested in this study. The unique binding site for U-92813 on GABAA receptors was confirmed by the insensitivity of its action to Ro 15-1788, a classical benzodiazepine antagonist, and by the additive nature of its agonistic activity with that of barbiturates and neurosteroids. With respect to the mechanism of potentiation, the pyrazinones are similar to the other allosteric modulators, in that they potentiate the GABA response more effectively at low GABA concentrations than at high GABA concentrations. We propose that substituted pyrazinones represent a novel class of allosteric modulators of GABAA receptors, with their binding site probably located between the alpha and beta subunits.

Allosteric Regulation↗

Allosteric modulators of metabotropic glutamate receptors: lessons learnt from mGlu1, mGlu2 and mGlu5 potentiators and antagonists.

Although relatively few G-protein-coupled receptors are Class C, in recent years, this small family of receptors has become a focal point for the discovery of new and exciting allosteric modulators. The mGlu (metabotropic glutamate) receptors are illustrative in the discovery of both positive and/or negative allosteric modulators with unique pharmacological properties. For instance, allosteric modulators of the mGlu2 receptor act as potentiators of glutamate responses in clonal expression systems and in native tissue assays. These potentiators act to increase the affinity of orthosteric agonists for the mGlu2 receptor and shift potency curves for the agonist to the left. In electrophysiological experiments, the potentiators show a unique activation-state-dependent presynaptic inhibition of glutamate release and significantly enhance the receptor-mediated increase in G-protein binding, as seen with autoradiography. Similarly, potentiators of mGlu5 have been described, as well as allosteric antagonists or inverse agonists of mGlu1 and mGlu5. Binding and activity of the modulators have recently indicated that positive and negative allosteric sites can be, but are not necessarily, overlapping. Compared with orthosteric ligands, these modulators display a unique degree of subtype selectivity within the highly conserved mGlu family of receptors and can have very distinct pharmacological properties, such as neuronal frequency-dependent activity. This short review describes some of the unique features of these mGlu1, mGlu2 and mGlu5 allosteric modulators.

Allosteric Regulation↗

Allosteric modulation of G protein-coupled receptors.

The past decade has witnessed a significant growth in the identification of allosteric modulators of G protein-coupled receptors (GPCRs), i.e., ligands that interact with binding sites that are topographically distinct from the orthosteric site recognized by the receptor's endogenous agonist. Because of their ability to modulate receptor conformations in the presence of orthosteric ligand, allosteric modulators can "fine-tune" classical pharmacological responses. This is advantageous in terms of a potential for engendering greater GPCR subtype-selectivity, but represents a significant challenge for detecting and validating allosteric behaviors. Although allosteric sites need not have evolved to accommodate endogenous ligands, there are a number of examples of where such modulators have been shown to contribute to physiological or pathophysiological processes. Studies are also beginning to unravel the structural basis of allosteric modulation of GPCRs. It remains to be determined whether such modulation represents interactions within monomers versus across dimers.

Allosteric Regulation↗

Allosteric modulation of GABA(B) receptor function in human frontal cortex.

In the present study, the effects of different allosteric modulators on the functional activity of gamma-aminobutyric acid (GABA)B receptors in membranes of post-mortem human frontal cortex were examined. Western blot analysis indicated that the tissue preparations expressed both GABA(B1) and GABA(B2) subunits of the GABA(B) receptor heterodimer. In [35S]-GTPgammaS binding assays, Ca2+ ion (1 mM) enhanced the potency of the agonists GABA and 3-aminopropylphosphinic acid (3-APA) and that of the antagonist CGP55845, but not that of the GABA(B) receptor agonist (-)-baclofen. CGP7930 (2,6-di-t-Bu-4-(3-hydroxy-2,2-dimethyl-propyl)-phenol), a positive allosteric modulator of GABA(B) receptors, potentiated both GABA(B) receptor-mediated stimulation of [35S]-GTPgammaS binding and inhibition of forskolin (FSK)-stimulated adenylyl cyclase activity. Chelation of Ca2+ ion by EGTA reduced the CGP7930 enhancement of GABA potency in stimulating [35S]-GTPgammaS binding by two-fold. Fendiline, also reported to act as a positive allosteric modulator of GABA(B) receptors, failed to enhance GABA stimulation of [35S]-GTPgammaS binding but inhibited the potentiating effect of CGP7930. The inhibitory effect was mimicked by the phenothiazine antipsychotic trifluoperazine (TFP), but not by other compounds, such as verapamil or diphenydramine (DPN). These data demonstrate that the function of GABA(B) receptors of human frontal cortex is positively modulated by Ca2+ ion and CGP7930, which interact synergistically. Conversely, fendiline and trifluoperazine negatively affect the allosteric regulation by CGP7930.

Adenylyl Cyclases↗

Phencyclidine is a negative allosteric modulator of signal transduction at two subclasses of excitatory amino acid receptors.

Phencyclidine (PCP) and some of its pharmacological congeners inhibit the signal transduction at specific excitatory amino acid receptors of cerebellar granule cells in primary cultures. These drugs do not bind to the transmitter recognition sites, and affinity of this specific binding site is increased by the presence of the transmitter bound to its recognition sites. PCP inhibits phosphatidylinositol phosphate hydrolysis mediated by Mg2+-sensitive glutamate receptors (GP1) but not that mediated by Mg2+-insensitive glutamate receptors (GP2). In addition, PCP inhibits Ca2+ influx and cGMP formation mediated by the activation of Mg2+-sensitive glutamate receptors (GC1) but not that mediated by Mg2+-insensitive glutamate receptors (GC2). In this cell culture the activation of phosphatidylinositol phosphate hydrolysis by muscarinic receptor agonists is not affected by PCP. Since PCP inhibits noncompetitively GP1 and GC1 signal transduction it may act as a negative allosteric modulator of signal transduction at both receptors. The pharmacological profile of PCP and its congeners delimits a class of drugs modulating allosterically the action of the primary transmitter at GP1 and GC1 receptors. These drugs need the presence of the transmitter to act and they cannot be termed inverse agonists because they are devoid of activity in the absence of the transmitter; moreover, they do not bind to the transmitter recognition site nor do they prevent the transmitter binding to its recognition sites.

Allosteric Regulation↗