Temperature, pH, and Molecular Packing Effects on the Penetration of Oleic Acid Monolayer by α-Lactalbumin

Recently, we reported on the interfacial behavior of mixed oleic acid (OA)-α-lactalbumin monolayer and its relevance in the formation of tumoricidal HAMLET (human α-lactalbumin made lethal to tumor cells)-like complex. This complex is probably formed in the gastrointestinal tract, but it has not been proved so far. The molecular base and the underlying physicochemical forces leading to such complexation remain to be known as well. There are also several other issues related with the complex stoichiometry that need to be fully explained. This study provides insight into the mechanism of temperature, pH, and physical state of monolayer-dependent binding of OA by the milk protein—apo-α-lactalbumin. Using the Langmuir and Langmuir–Blodgett approaches, we investigated the interactions between the OA monolayer and the apo-bovine α-lactalbumin (BLA III) at different pH, temperatures, and molecular packing. We found that the most favorable conditions for the formation of mixed OA–BLA III film are relevant to the ...