OH-Radical Oxidation of Lung Surfactant Protein B on Aqueous Surfaces

Air pollutants generate reactive oxygen species on lung surfaces. Here we report how hydroxyl radicals (·OH) injected on the surface of water react with SP-B_1-25, a 25-residue polypeptide surrogate of human lung surfactant protein B. Our experiments consist of intersecting microjets of aqueous SP-B_1-25 solutions with O₃/O₂/H₂O/N₂(g) gas streams that are photolyzed into ·OH(g) in situ by 266 nm laser nanosecond pulses. Surface-sensitive mass spectrometry enables us to monitor the prompt (<10 μs) and simultaneous formation of primary O -containing products/intermediates (n≤5) triggered by the reaction of ·OH with interfacial SP-B_1-25. We found that O-atoms from both O₃ and ·OH are incorporated into the reactive cysteine Cys₈ and Cys₁₁ and tryptophan Trp₉ components of the hydrophobic N-terminus of SP-B_1-25 that lies at the topmost layers of the air-liquid interface. Remarkably, these processes are initiated by ·OH additions rather than by H-atom abstractions from S-H, C-H, or N-H groups. By increasing the hydrophilicity of the N-terminus region of SP-B_1-25, these transformations will impair its role as a surfactant.