BSA/ HAS interaction and antioxidant evaluation of newly synthesized benzoxazine Derivatives: Spectrophotometric and molecular docking studies

BSA and HSA binding activity of recently reported benzoxazine derivatives (BD) was studied at 298.15 K with UV/Vis, fluorescence spectrophotometric and docking analysis. In spectrophotometric method, BDs at 260 nm (λmax) has shown hypo chromic effect inferring intercalating nature of BDs. The Fluoro substitution at para position have been found most effectively due to providing conventional hydrogen binding between itself and hydrogen of proteins. The fluorescence quenching experiments revealed the formation of non-fluorescent complex inferring interaction of BDs and proteins. Scatchard parameters showed four and six binding sites available in BSA and HSA respectively, during interaction with BDs, where higher value of Kb suggests that higher binding strength of HSA as compared to BSA. The docking analysis inferred the conventional hydrogen bonding and hydrophobic-hydrophobic interaction due to presence of fluoro and alkyl groups in BDs respectively. Protein binding activity of BDs proved their medicinal potential specially in cancer treatment. Their antioxidant (AOA) activity proved their medicinal importance by showing more than 70% radical scavenging.