PLASMA-PROTEIN BINDING OF GYRASE INHIBITORS

Plasma protein binding of a wide range of gyrase inhibitors in clinica l practice or trials has been determined by ultrafiltration to determi ne structure-protein binding relationships. The protein binding was in dependent of overall lipophilicity. In particular, the ''western'' par i of the ''quinolone'' skeleton, consisting of a heterocyclus at posit ion 7 and varying substituents at position 8, strongly influences the extent of protein binding, indicating that this part interacts with th e plasma protein. In contrast, substituents in position N-1 do not sho w an effect on the protein binding in this series of compounds.