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 bee...

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Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 35(2019), 8 vom: 26. Feb., Seite 3183-3193
Auteur principal: Krajewska, Martyna (Auteur)
Autres auteurs: Dopierała, Katarzyna, Weiss, Marek, Prochaska, Krystyna
Format: Article en ligne
Langue:English
Publié: 2019
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, Non-U.S. Gov't Aluminum Silicates Oleic Acid 2UMI9U37CP Lactalbumin 9013-90-5 mica V8A1AW0880
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520 |a 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 gastric environment. The stabilization of OA-BLA III at the interface is associated with the conformational changes of protein in the presence of fatty acids induced by low pH and high temperature in the expanded monolayer. Our approach helps to understand the molecular mechanism of HAMLET/bovine α-lactalbumin made lethal to tumor cells formation in vivo 
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