Interaction between quinolones antibiotics and bacterial outer membrane porin OmpF.
In these work, we try to establish a relation between the hydrophobicity of some quinolones and their interaction with OmpF. In order to do that, the values of the binding constant of some quinolones of different "generations" with OmpF were determined by UV-visible spectrophotometry and by fluorimetry.  Our results show that there is a strong interaction between all the drugs and the protein and that it becomes larger for the last "generation" fluoroquinolones.  These results were compared with previous ones obtained for the interaction of these drugs with simpler biomembrane models (liposomes) and it is possible to conclude that some of the quinolones associate preferably with the protein than with these models.  This suggests that an interaction drug/porin is, probably, the preferentially used for the latest fluoroquinolones what makes reasonable to believe that a strong affinity for OmpF means a better capacity to transpose the barrier formed by the outer membrane.