Ethanol binding to a model carbohydrate, glycogen.

The binding affinity of ethanol for carbohydrates is unknown. Glycoconjugates are postulated to be sensitive targets of ethanol action. The glycogen content of muscle, liver, and brain is sensitive to ethanol. To explore whether carbohydrates as a class have a specific affinity to bind ethanol, we measured the binding of ethanol and other small molecules to the carbohydrate glycogen. Ethanol binding was found to be weak. The polar alcohol, glycerol, bound to glycogen with a greater affinity than ethanol did. Other small polar molecules (methanol, sucrose, acetate, glycine, and dimethyl sulfoxide) also bound more strongly than ethanol did. Ethanol and glycerol binding were concentration independent. No evidence of saturable or specific sites for these alcohols was obtained. Water binding was determined and was in agreement with hydrodynamic measures. Water binding exceeded the binding of all solutes studied. The loosely structured water of hydration in glycogen apparently was able to accommodate polar solutes, but tended to exclude ethanol and, to a lesser extent, methanol. We conclude that carbohydrates as a class exhibit no strong affinity or specificity for ethanol.