RESUMEN
Photoallergy is a photosensitivity disorder associated with a modified ability of the skin to react to the combined effect of drugs and sunlight. It has been attributed to the covalent conjugation of proteins with a photosensitizer, yielding modified macromolecules that can act as antigen provoking the immune system response. The potential role of some endogenous compounds as photoallergens has not been fully established. It has been previously proposed that pterins, which are endogenous photosensitizers present in human skin under pathological conditions, are able to covalently bind to proteins. Here, we evaluated the capability of pterin (Ptr) to form photoadducts with free Lysine (Lys) and poly-L-lysine (poly-Lys). The findings obtained using chromatographic and spectroscopic tools, confirm the formation of photoadducts of Ptr with Lys residues. With poly-Lys the resulting adduct retains the spectroscopic properties of the photosensitizer, suggesting that the aromatic Ptr structure is conserved. On the other hand, the photoproduct formed with free Lys does not behave like Ptr, which suggests that if this product is a photoadduct, a chemical modification may have occurred during the photochemical reaction that alters the pterin moiety.