Blood proteins are the main factors for the transportation and homing of drugs to the target molecules 1, 2, 3. Bioavailability of the drug under testing is important for its direct regulation, interaction and involvement in immunity generation and metabolism. The protein contents of body fluids are considered to be a vital index for the clinical diagnosis of any drug. This study suggests optimal efficiency of diffusion of the BrNs into the bloodstream for the treatment of cancer.
Molecular dynamics simulation analysis also suggested the stable binding with lower deviation in RMSD and RMSF values through persistent long simulation run. Molecular docking showed strong interactions with score of −8.08 kcal/mol. The in vitro findings were further confirmed by in silico assays. Moreover, results of FT-IR, CD, UV spectra concluded significant conformational change in BSA on binding with BrNs. Based on thermodynamic analysis, it was deduced that binding process of the BrNs with BSA was spontaneous and exothermic, and the major forces between BrNs and BSA were van der waals forces and hydrogen bonding. The stoichiometry of BrNs-BSA complex was 1:1 and binding constant of the complex was in the order of 10 3 M −1 at 298 K. The intrinsic fluorescence of BSA was quenched by BrNs through a static quenching procedure. Here, various spectroscopic techniques and computational methods were employed to understand the dynamics of BrNs and BSA interaction.
The mechanistic interaction insight into the binding of bovine serum albumin (BSA) with BrNs can provide critical information about the pharmacodynamics and pharmacokinetics properties. Bromo-Noscapine (BrNs) is a tubulin-binding cytotoxic agent with significant activity against breast and lung cancer.
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