Thermodynamics of the binding of salicylate to human serum albumin: evidence of non-competition with imidazole

Abstract

Abstract The thermodynamic characteristics of the binding of salicylate to human serum albumin have been studied using a technique based on the variation of the quantum yield of fluorescence of salicylate when it binds to the protein. The binding constants, number of sites and the values of ΔG°, ΔH° and Δ° were determined. The results are consistent with a model that proposes two equal and independent types of binding site with a predominantly ionic interaction and an important hydrophobic contribution in one of the sites. The technique was also used to demonstrate that imidazole and salicylate (that can be found simultaneously in plasma following administration of imidazole-2-hydroxybenzoate) do not compete for the same binding sites on the protein.