Molecular docking analysis on the interaction between bovine serum albumin and three commercial fluoroquinolones: Ciprofloxacin, enrofloxacin and pefloxacin

Abstract

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%.

Interaction of Ibuprofen with Partially Unfolded Bovine Serum Albumin in the Presence of Ionic Micelles and Oligosaccharides at Different λex and pH: A Spectroscopic Analysis

“… 10 The secondary structure of BSA consists of 67% α-helix and 10% turn configurations without any β-sheets, while its tertiary structure is composed of three domains (I, II, and III), and each consists of two subdomains (A and B). 11 BSA is structurally homologous to protein human serum albumin (HSA), both of which are alike in terms of ligand binding affinity and share almost 80% sequence homology. 12 There are two tryptophan (Trp) residues present in BSA, Trp-134 and Trp-212; Trp-134 is located on the surface of domain IB, whereas Trp-212 is located in the hydrophobic pocket of subdomain IIA; thus, the microenvironment around Trp-134 is more polar than that around Trp-212.…”

“…10 The secondary structure of BSA consists of 67% α-helix and 10% turn configurations without any β-sheets, while its tertiary structure is composed of three domains (I, II, and III), and each consists of two subdomains (A and B). 11 BSA is structurally homologous to protein human serum albumin (HSA), both of which are alike in terms of ligand binding affinity and share almost 80% sequence homology. 12 Trp-212.…”

“…It belongs to the class of SAs which are considered the most important plasma proteins as they play pivotal roles in drug delivery due to their ability to reversibly bind to therapeutic molecules and act as carriers for various fatty acids, amino acids, bile salts, metal ions, hormones, and drugs . The secondary structure of BSA consists of 67% α-helix and 10% turn configurations without any β-sheets, while its tertiary structure is composed of three domains (I, II, and III), and each consists of two subdomains (A and B) . BSA is structurally homologous to protein human serum albumin (HSA), both of which are alike in terms of ligand binding affinity and share almost 80% sequence homology .…”