Luminescencence determination of ecotoxicants in protein-based media

Abstract

The structural changes in the protein macromolecules caused by polycyclic aromatic hydrocarbon (PAH) ecotoxicants were studied using the data on intrinsic fluorescence of proteins and fluorescence of PAH molecules introduced into proteins. A luminescence method for PAH determination in proteins was developed and used to study the interaction of two PAHs (pyrene and anthracene) with proteins of two types (bovine serum albumin and human serum albumin). The results were interpreted using the Stern–Volmer fluorescence quenching model. The association constants and the number of binding sites in the protein–ligand complexes were calculated. The binding of PAHs with proteins was described based on the static version of quenching with formation of nonfluorescent complexes of protein fluorophores with PAHs.