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Disruption of pulmonary surfactant function under oxidative stress: structural and biophysical insights

Citation

Cejas, J. d. P., Cañadas, Ledesma, Rosa, Collada, Blanco-Rivero, Pérez-Gil, Disalvo, & Frías, M. d. l. A. (2026). Disruption of pulmonary surfactant function under oxidative stress: structural and biophysical insights. Journal of Colloid and Interface Science, 716. https://doi.org/10.1016/J.JCIS.2026.140353

Abstract

Pulmonary surfactant forms surface-active films at the air-liquid interface which are essential for alveolar stability but are highly susceptible to oxidative damage under inflammatory conditions. The reactive species hypochlorous acid (HClO/ClO−), generated by activated neutrophils, is a potent oxidant that may compromise surfactant integrity; however, its molecular and functional impact remains incompletely understood. In this study, the effects of oxidative stress induced by HClO/ClO− on the biophysical and structural properties of a fully native porcine surfactant were investigated using Langmuir balance, captive bubble surfactometry, differential scanning calorimetry, FTIR-ATR spectroscopy, and epifluorescence microscopy. Oxidation induced concentration- and time-dependent inhibition of surfactant adsorption and interfacial film stability. Langmuir balance experiments revealed selective disruption of films containing unsaturated phospholipids or native mixtures, while saturated monolayers remained largely unaffected. FTIR-ATR analysis showed perturbations in lipid headgroup regions and protein secondary structure rearrangements towards β-sheet-rich aggregates, consistent with oxidative unfolding and aggregation. These molecular changes compromise protein-lipid interactions, delaying adsorption and respreading at the air-liquid interface. Epifluorescence microscopy further revealed disruption of lateral lipid organization and altered formation of three-dimensional surfactant reservoirs enriched in disordered components. Functional assays confirmed impaired reduction of surface tension during quasi-static cycling, partially alleviated under dynamic cycling, suggesting exclusion or depuration of oxidized components from the interface. Together, these findings demonstrate that neutrophil-derived oxidants progressively compromise pulmonary surfactant by targeting lipid-protein cooperativity, leading to early interfacial dysfunction followed by structural reorganization. This mechanistic insight advances understanding of oxidative surfactant inactivation and supports the development of antioxidant strategies or oxidant-resistant surfactant formulations as potential therapeutic interventions for inflammatory lung injury.

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The authors acknowledge funding by the Spanish Ministry of Science and Innovation (grant no. PID2024-156556OB-I00 to JPG) and by CONICET PIP 2021-2023 N° 2433 to MAF.

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