In this work, three compounds having the same organic moiety (N-methyl-5-azahelicenium salts) but different counterions (I-, NO3- and COOCF3-) have been investigated in buffered aqueous solutions and in the presence of DNA to give information on the counterion effects on the binding. In particular, the absorption spectra, fluorescence quantum yields and fluorescence lifetimes in aqueous solution for free organic molecules have been determined by steady-state and time-resolved spectrofluorimetric measurements. The obtained values are compared with those of the chromophores in the presence of increasing concentrations of DNA. The results allow determination of the association constants (K(a)) and the number of base couples per chromophore molecule (n) by means of the McGhee Von Hippel model. The binding parameters are strongly affected by the nature of counterions since the highest K(a) value was determined for the compound having COOCF3-; on the other hand the NO3- derivative is able to interact with the highest number of binding sites. The morphology and structural properties of the DNA-chromophore complexes were investigated by circular dichroism (CD) and atomic force microscopy (AFM). The data revealed that I- and COOCF3- derivatives preferentially form intercalation complexes, while the NO3- salt is able to form intercalation and grove binding complexes at the same time.

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Photosensitized protein oxidation by drugs, with the consequent modification of their structure is thought to be responsible for the occurrence of phototoxic phenomena such as photoallergy and loss of biological functions. In this paper we have investigated in detail the interaction of four fluoroquinolones namely ciprofloxacin, lomefloxacin, norfloxacin and ofloxacin with two proteins such as Bovine Serum Albumin (BSA) and Ribonuclease A (RNAse A) chosen as models. The interactions between the four drugs and the proteins, were studied by absorption and emission spectroscopy. Photophysical experiments were carried out in aqueous solutions by stationary and time-resolved fluorimetry and by laser flash photolysis, in the absence and in the presence of the proteins to obtain information on the various decay pathways of the excited states of the drugs and on transient species formed upon irradiation. In parallel we have investigated by a series of biochemical assays the photoinduced modifications exerted by the four drugs. The obtained results showed that the four drugs are able to photooxidize proteins with the formation of protein-protein cross-link. This effect was also confirmed in isolated erythrocyte membranes. Furthermore the effect of the fluoroquinolones was also evaluated on isolated aromatic aminoacids. In this context the four drugs are able to photodamage in particular tyrosine and histidine. These results are important in the light of the growing interest for the comprehension of the mechanism of phototoxicity induced by these antibacterial drugs.