Structure and wettability of heterogeneous monomolecular films of phospholipids with cholesterol or lauryl gallate

Jurak, Małgorzata; Mroczka, Robert; Łopucki, Rafał; Wiącek, Agnieszka Ewa

doi:10.1016/j.apsusc.2019.07.065

Cited by 4 publications

(1 citation statement)

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“…Therefore, a model system mimicking a biological membrane environment is utilized to facilitate an in-depth understanding of the intermolecular interactions between proteins and phospholipids at the interface. The study of protein–lipid interactions at an interface can usually be performed in a controlled way by the Langmuir–Blodgett (LB) technique, − and the Langmuir monolayers ,, are frequently used as a model system for a better understanding of the interfacial behavior of a protein within a biological system …”

Section: Introductionmentioning

confidence: 99%

Interfacial Interactions of a Myoglobin/DOPC Hybrid System at the Air–Water Interface and Its Physicochemical Properties

Ahmed,

Das,

Islam

et al. 2023

ACS Omega

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In the present study, the intermolecular interactions between a water-insoluble phospholipid (DOPC) and watersoluble protein (myoglobin) and the interaction among themselves were investigated at the air−water interface using the Langmuir and Langmuir−Blodgett techniques. The effects of changes in physicochemical factors, like pH and temperature, on these interactions were also examined. Surface pressure−molecular area (π−A) isotherms of the DOPC monolayer at the air−water interface, with and without myoglobin (Myo) revealed the evolution of various physical properties, such as elastic, thermodynamic, and hysteric properties, in response to changes in subphase pH and temperature. With the increment of subphase pH from 5 to 7 at a fixed temperature (20 °C), the DOPC isotherm expanded, and the in-plane elasticity (C S −1) decreased, but no significant presence of hysteresis was encountered in either of the pH values. On the other hand, a diminution of temperature (from 20 to 5 °C) leads to an expansion of monolayers yielding low elasticity and significant hysteresis. The incorporation of Myo molecules within the DOPC monolayer decreased the C S −1 value of the DOPC monolayer. Such a decrement in C S −1 was also encountered while increasing the pH and decreasing the temperature (T) of the subphase in the absence of Myo. Systematic expansion of DOPC isotherm and increased hysteric area with the increase in Myo proportion were observed and the atomic force microscopy (AFM) observations suggested a strong conjugation between Myo and DOPC in the mixed monolayer. The denaturation effect of Myo molecules was studied using AFM at different temperatures. Furthermore, the Myo molecules were found to be most surface active at pH = 7, which is very close to its isoelectric point. These observations come up with the interaction mechanism between biomolecules under dynamically varied conditions.

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