The photoreactivity of naphazoline (NP), 2-(1-naphthylmethyl)imidazoline, i
n the presence of bovine serum albumin (BSA) is investigated. The protein m
icroenvironment affects markedly the efficiency of the photochemical deacti
vation pathways of the NP transient intermediates photogenerated upon laser
excitation. The triplet state of the drug associates with BSA and its life
time increases by more than one order of magnitude. Hydrated electrons and
nitrogen-centered radicals formed in the NP photolysis react efficiently wi
th protein sites, behaving as sources of reductive and oxidative protein da
mage, respectively. NP photoinduced protein structural modification is also
observed.