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Short-chain alcohols inhibited the equilibrium binding of agonists and antagonists to rat heart muscarinic receptors. Methanol, ethanol, propan-2-ol and propan-1-ol, when used at low concentrations, behaved as pseudo-competitive antagonists. Their rank order of potency paralleled their relative partition coefficients, suggesting that this inhibition was simply due to the interaction of the alcohols with a hydrophobic part of the receptor or with membrane lipids. The four alcohols increased the dissociation rate constant of [3H]oxotremorine M from the high-affinity agonist receptors and decreased the stability of this receptor state. These effects might reflect increased membrane fluidity and/or decreased hydrophobic interactions (see below). By contrast, the effects of alcohols on the association and dissociation rates of N-[3H]- methscopolamine (an antagonist) were not correlated to their relative octanol/water partition coefficient (a measure of their affinity for biophases ). Alcohols, at the relatively high concentrations necessary for increased membrane 'fluidity', are known to affect the relative stability of various protein conformations. We believe that the effects of alcohols on antagonist binding to rat heart muscarinic receptors reflected changes in the activation energy of association and dissociation reactions, the inhibition of equilibrium binding being mainly due to decreased 'hydrophobic interactions'.

Multiple effects of short-chain alcohols on binding to rat heart muscarinic receptors