Preventing the adsorption of serum proteins to the alveoli air/aqueous interface becomes an important issue since blood serum proteins inactivate the lung surfactant mixture by adsorbing in a faster and irreversible way. As a result of this phenomenon, respiration may not be performed regularly and fatal diseases such as Acute Respiratory Distress Syndrome (ARDS) occur. ARDS is a mortal disease, which cannot be treated effectively. Although some treatments are applied, usages of synthetic surfactants, which can resist to surfactant inactivation, are still expected to be improved. Considering that respiration is a very rapid and continuous process, dynamic behaviors and interfacial properties of alternative medicines under development and their interactions with blood proteins are extremely important. In this study, dynamic adsorption behaviors, interfacial properties and interactions of the newly designed CF3(CF2)7SO3-(CH2CH3)3N+(CH2OCH2)10(CH2)15CH3), (IPL) with lung surfactant and fibrinogen, the most problematic serum protein, are investigated with various experimental setups. IPL is designed to be simple yet effective by considering the function-structure relationship of the molecule. Owing to its functional segments IPL is a unique molecule that possesses important properties such as mimicking the lung surfactant protein B. It is able to mix and interact synergistically with DPPC -the most abundant lipid in the lung surfactant mixture- and enhance its dynamic adsorption and interfacial properties. Parallel to dynamic adsorption results obtained from pendant drop measurements, Langmuir trough experiments have shown that by the inclusion of IPL at the interface, adsorption of fibrinogen is significantly prevented. Moreover, lipid loss from the interface due to fibrinogen adsorption is substantially decreased and the negative effect of fibrinogen on the hysteresis behavior of natural lung surfactant is improved when IPL is presented at the interface. All results indicate that IPL provides promising results in terms of preventing the fibrinogen adsorption and resisting to surfactant inactivation.

Sustaining a healthy respiration by preventing the adsorption of blood protein: Effect of novel ion pair surfactant

246th National Meeting (2013)

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