Cation dependence of opioid receptor binding supports theory on membrane-mediated receptor selectivity

Abstract
A quantitative analysis of the binding of dynorphin A-(1-9)-nonapeptide to the opioid .kappa.-receptors of the guinea pig cerebellum [Paterson et al. (1986) Proc. Natl. Acad, Sci. U.S.A. 83, 6216-6220] shows that changes in electrostatic surface accumulation of the ligand fully account for the observed suppression of binding by a series of univalent and divalent salts. Binding to .mu.- and .delta.-receptors, on the other hand, is subject to additional ion-specific effects. These observations support the membrane locations for the receptor sites proposed by the "membrane compartments" theory for opioid receptor selection.

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