Among numerous compounds found in marine organisms, triterpenes have attracted considerable research interest due to a beneficial impact on health including anti-inflammatory, antitumor, antiviral, and antioxidation effects. Specifically, new functionalities of oleanolic acid (OLA) have been revealed recently, indicating possible applications in nutrition and pharmaceuticals. However, this bioactive material has limited value due to low water solubility and stability. Therefore, oleanolic acid needs a carrier that protects it and enables controlled release in the human body. Innovative drug delivery systems provide a promising strategy for overcoming these problems. However, the development of those systems requires a comprehensive understanding of the physicochemical properties of triterpenes and their carriers as well as the interactions between them. Among numerous substances, human serum albumin (HSA) has been widely studied as a drug carrier. In addition, human serum albumin is the main blood plasma protein responsible for the transport of drugs and metabolites; therefore, the interactions between that protein and other substances are of physiological and pharmaceutical importance. Moreover, sensing the HSA level in blood plasma is an important challenge that requires binding studies on a molecular scale. The aim of this study was to investigate the properties of oleanolic acid in the presence of human serum albumin in terms of thermodynamics, morphology, and viscoelasticity at the air/water interface. Moreover, the wettability, surface free energy, and topography of the films after deposition on the solid substrate were determined. The results have been discussed in terms of providing physicochemical insight into the interfacial behavior of the OLA–HSA complex, which is crucial for pharmaceutical and bioanalytical applications.
In the Langmuir monolayer technique, a single layer of molecules is formed on a water subphase. This approach was used to mimic the antitumoricidal lipid–protein complex of oleic acid and bovine α-lactalbumin called the BAMLET complex. Our previous studies have shown that at the interface, the BAMLET complex is stabilized by the hydrophobic forces supported by the hydrogen bonds. This study provides an insight into the influence of calcium ions and the experimental conditions (temperature and subphase pH) on the stability of the complex at the interface. The Langmuir technique was expanded using a dosing pump to exchange the subphase and deliver additional substances to the system. We investigated the interactions between oleic acid monolayer and α-lactalbumin in the presence of Ca2+ in the bulk and the effect of varied experimental conditions on the complex stability. The role of calcium ions in this system is important because (in addition to low pH and relatively high temperature) it affects the conformational changes within the protein molecule and facilitates the transition of α-lactalbumin into the molten globule state. A partially unfolded state is required to form the BAMLET complex. We found that the mixed monolayer spread at the interface is stable despite drastic changes in the process conditions and remains stable even after the subphase exchange. This study of molecular interactions explored by the Langmuir technique with peristaltic pump enabled to understand the role of Ca2+ in BAMLET complex formation.
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 proteinapo-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.
We report a novel stimuli-responsive fluorescent material platform that relies on an evocation of aggregationinduced emission (AIE) from tetraphenylethylene (TPE)-based surfactants localized at one hemisphere of biphasic microscale Janus emulsion droplets. Dynamic alterations in the available interfacial area were evoked through surfactantinduced dynamic changes of the internal droplet morphology that can be modulated as a function of the balance of interfacial tensions of the droplet constituent phases. Thus, by analogy with a Langmuir-Blodgett trough that enables selective concentration of surfactants at a liquid-gas inter-face, we demonstrate here a method for controllable modulation of the available interfacial area of surfactantfunctionalized liquid-liquid interfaces. We show that a morphology-dependent alteration of the interfacial area can be used to evoke an optical signal, by selectively assembling synthesized TPE-based surfactants on the respective droplet interfaces. A trigger-induced increase in the concentration of TPE-based surfactants at the liquid-liquid interfaces results in an evocation of aggregation-induced emission (AIE), inducing an up to 3.9-fold increase in the measured emission intensity of the droplets.
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