Fluoroquinolones are a family of broad spectrum, systemic antibacterial agents that have been used as therapy for infections in the respiratory and alimentary tract in animals. The pharmacodynamic of this class is widely described, predominantly to the commercial drugs ciprofloxacin (CIP), enrofloxacin (ENR), and pefloxacin (PEF). Bovine serum albumin (BSA) is the main endogenous carrier in the bovine bloodstream, being responsible for the biodistribution of different classes of molecules and drugs, including fluoroquinolones. The molecular features and interaction between BSA and fluoroquinolones are not fully described, thus, the present work enlightens the intimacy of the interaction of BSA with CIP, ENR, PEF through structural modeling and molecular docking calculation approaches. The role of key amino acid residues was assessed, indicating that the main protein binding pocket is composed by Trp-212 residue playing an important stabilization for the three fluoroquinolones through both hydrogen bonding and van der Waals forces, where reside the individual structural differences observed among the three fluoroquinolones and BSA. There is a descriptive protagonism of carboxyl group on the ENR interaction which traps the molecule and avoids the deep communication in the protein binding pocket, as well as the ligands CIP and PEF showed an interface amino acid residue interaction profile higher than 70%.
Protein binding of sulfonylureas. I. Interaction of some substituted benzenesulfonyl propylureas to bovine serum albumin.