1 research outputs found
Protein Cross-Linking and Oligomerization through Dityrosine Formation upon Exposure to Ozone
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 (O<sub>3</sub>) exposure were studied in coated-wall flow tube experiments at environmentally
relevant O<sub>3</sub> 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 O<sub>3</sub> in the Anthropocene may promote the formation of protein oligomers
with enhanced allergenicity and may thus contribute to the increasing
prevalence of allergies