Pollen allergy represents a growing public health concern, yet the role of microplastic pollution in modulating allergen behavior remains largely unresolved. In this study, we investigated interactions between polyethylene terephthalate (PET) microplastics (0.2–12 µm; predominantly 0.4–1 µm) and cedar pollen proteins, with emphasis on the major allergen Cry j 1. Surface charge characterization using the pH drift method revealed two apparent points of zero charge in the acidic (pH 3.0–3.8) and near-neutral (~7.5) regions, indicating surface chemical heterogeneity. Protein adsorption experiments conducted at physiological pH (7.4) showed concentration-dependent and saturable removal of proteins from solution with increasing PET mass and a 3.10-fold preferential enrichment of aromatic-rich protein fractions. Spectroscopic analyses revealed adsorption-induced but non-denaturing structural perturbations, including increased exposure of aromatic residues and partial β-sheet destabilization. Complementary all-atom molecular dynamics simulations showed rapid and stable Cry j 1 adsorption onto PET, anisotropic surface accommodation, modest increases in solvent accessibility, and subtle secondary structure rearrangements without global unfolding. Together, these findings indicate that PET microplastics can selectively bind and structurally modulate pollen allergens in ways that may influence allergen persistence and epitope presentation, with potential implications for IgE-mediated sensitization in polluted environments.
Maduka et al. (Wed,) studied this question.