Air pollution and climate change are potential drivers for the increasing burden of allergic diseases. The molecular mechanisms by which air pollutants and climate parameters may influence allergic diseases, however, are complex and elusive. This article provides an overview of physical, chemical and biological interactions between air pollution, climate change, allergens, adjuvants and the immune system, addressing how these interactions may promote the development of allergies. We reviewed and synthesized key findings from atmospheric, climate, and biomedical research. The current state of knowledge, open questions, and future research perspectives are outlined and discussed. The Anthropocene, as the present era of globally pervasive anthropogenic influence on planet Earth and, thus, on the human environment, is characterized by a strong increase of carbon dioxide, ozone, nitrogen oxides, and combustion- or traffic-related particulate matter in the atmosphere. These environmental factors can enhance the abundance and induce chemical modifications of allergens, increase oxidative stress in the human body, and skew the immune system toward allergic reactions. In particular, air pollutants can act as adjuvants and alter the immunogenicity of allergenic proteins, while climate change affects the atmospheric abundance and human exposure to bioaerosols and aeroallergens. To fully understand and effectively mitigate the adverse effects of air pollution and climate change on allergic diseases, several challenges remain to be resolved. Among these are the identification and quantification of immunochemical reaction pathways involving allergens and adjuvants under relevant environmental and physiological conditions.

We found that ambient and laboratory-generated secondary organic aerosols (SOA) form substantial amounts of OH radicals upon interaction with liquid water, which can be explained by the decomposition of organic hydroperoxides. The molar OH yield from SOA formed by ozonolysis of terpenes (α-pinene, β-pinene, limonene) is ∼ 0.1 % upon extraction with pure water and increases to ∼ 1.5 % in the presence of Fe²⁺ ions due to Fenton-like reactions. Upon extraction of SOA samples from OH photooxidation of isoprene, we also detected OH yields of around ∼ 0.1 %, which increases upon addition of Fe²⁺. Our findings imply that the chemical reactivity and aging of SOA particles is strongly enhanced upon interaction with water and iron. In cloud droplets under dark conditions, SOA decomposition can compete with the classical H₂O₂ Fenton reaction as the source of OH radicals. Also in the human respiratory tract, the inhalation and deposition of SOA particles may lead to a substantial release of OH radicals, which may contribute to oxidative stress and play an important role in the adverse health effects of atmospheric aerosols.

Hydroxyl radical-induced oxidation of proteins and peptides can lead to the cleavage of the peptide, leading to a release of fragments. Here, we used high-performance liquid chromatography tandem mass spectrometry (HPLC-MS/MS) and pre-column online ortho-phthalaldehyde (OPA) derivatization-based amino acid analysis by HPLC with diode array detection and fluorescence detection to identify and quantify free amino acids released upon oxidation of proteins and peptides by hydroxyl radicals. Bovine serum albumin (BSA), ovalbumin (OVA) as model proteins, and synthetic tripeptides (comprised of varying compositions of the amino acids Gly, Ala, Ser, and Met) were used for reactions with hydroxyl radicals, which were generated by the Fenton reaction of iron ions and hydrogen peroxide. The molar yields of free glycine, aspartic acid, asparagine, and alanine per peptide or protein varied between 4 and 55%. For protein oxidation reactions, the molar yields of Gly (∼32–55% for BSA, ∼10–21% for OVA) were substantially higher than those for the other identified amino acids (∼5–12% for BSA, ∼4–6% for OVA). Upon oxidation of tripeptides with Gly in C-terminal, mid-chain, or N-terminal positions, Gly was preferentially released when it was located at the C-terminal site. Overall, we observe evidence for a site-selective formation of free amino acids in the OH radical-induced oxidation of peptides and proteins, which may be due to a reaction pathway involving nitrogen-centered radicals.

Cerium dioxide nanoparticles and nanorods were found to exhibit much stronger scavenging activity than ·OH generation in quasi-physiological conditions.