Sebacic (decanedioic) acid is a dicarboxylic acid proposed recently as an alternative energy substrate in total parenteral nutrition. In this paper, binding of sebacic acid to defatted human plasma albumin, also in the presence of decanoic acid, was studied by means of equilibrium dialysis. In addition, the binding of sebacic acid in human serum was investigated. Binding to defatted albumin was analysed by a model with two independent classes of sites with different affinity constants. The fitting procedure took into account some of the measurement errors that are likely to affect the equilibrium dialysis technique. We found for sebacic acid one binding site with affinity constant 3.69 x 10(4) M-1 and four to five sites with affinity constant 7.14 x 10(2) M-1. Association constants for decanoic acid are 3-4-fold larger than those of sebacic acid. Data of binding of sebacic acid in human serum suggested that only three to five of the low affinity sites are available for binding. When disodium sebacate is administered i.v. for total parenteral nutrition, a substantial fraction of sebacic anions is likely to be bound in serum.