Protein modifications may occur upon exposure to environmental toxins such as polycyclic aromatic hydrocarbon (PAH) molecules or their metabolites. In this context, our laboratory was interested in investigating protein modifications in the presence of select naphthoquinones, which were 2-hydroxy-1,4-naphthoquinone (HNQ) and 1,2-naphthoquinone (o-NQ). The effects of HNQ and o-NQ on the protein Ribonuclease A (RNase) were investigated through a variety of conditions. These modified incubation conditions included pH variation and the addition of metal ions to further mimic physiological conditions. Documentation of results was carried out through sodium dodecyl sulfate polyacrylamide gel electrophoretic analysis (SDS-PAGE). Of the two quinones, o-NQ exhibited a greater level of activity toward RNase. HNQ was found to be stable under the studied conditions, resulting in almost no observed RNase modification. Linking environmentally abundant compounds to toxicological effects on biologically significant molecules can help to set precedents toward their usage and disposal that have a positive ripple effect
