Physicochemical Properties of Some Semisynthetic Penicillins

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Abstract
Variation in the structure of the sidechain of penicillins has been shown to be associated with changes in the physicochemical properties of the substances. Values obtained for ionization constants, oleyl alcohol/water partition coefficients, and binding to serum albumin in a series of 10 semisynthetic penicillins varied from 2.78 to 5.41, from 0.87 to > 800, and from 29% to 100%, respectively. The partition coefficient appears to be the most important of these parameters. Decrease in acid strength is due probably to the formation of dimers by highly nonpolar penicillins. Increase in extent of binding to albumin has been shown previously to be due to increase in hydrophobic bonding between highly nonpolar penicillins and the protein surface. Our data support this. In certain cases, the formation of reinforced ionic bonds may supplement nonionic bonding.

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