Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone.
- Author(s): Kampf, Christopher J
- Liu, Fobang
- Reinmuth-Selzle, Kathrin
- Berkemeier, Thomas
- Meusel, Hannah
- Shiraiwa, Manabu
- Pöschl, Ulrich
- et al.
Published Web Locationhttps://doi.org/10.1021/acs.est.5b02902
Air pollution is a potential driver for the increasing prevalence of allergic disease, and post-translational modification by air pollutants can enhance the allergenic potential of proteins. Here, the kinetics and mechanism of protein oligomerization upon ozone (O3) exposure were studied in coated-wall flow tube experiments at environmentally relevant O3 concentrations, relative humidities and protein phase states (amorphous solid, semisolid, and liquid). We observed the formation of protein dimers, trimers, and higher oligomers, and attribute the cross-linking to the formation of covalent intermolecular dityrosine species. The oligomerization proceeds fast on the surface of protein films. In the bulk material, reaction rates are limited by diffusion depending on phase state and humidity. From the experimental data, we derive a chemical mechanism and rate equations for a kinetic multilayer model of surface and bulk reaction enabling the prediction of oligomer formation. Increasing levels of tropospheric O3 in the Anthropocene may promote the formation of protein oligomers with enhanced allergenicity and may thus contribute to the increasing prevalence of allergies.