Abstract
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 O(3)/O(2)/H(2)O/N(2)(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 (n) -containing products/intermediates (n≤5) triggered by the reaction of ·OH with interfacial SP-B(1-25). We found that O-atoms from both O(3) and ·OH are incorporated into the reactive cysteine Cys(8) and Cys(11) and tryptophan Trp(9) 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.