Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking

Abstract

This article presents the binding interaction between mebendazole (MBZ) and bovine serum albumin. The interaction has been studied using different techniques, such as fluorescence quenching spectroscopy, UV–visible spectroscopy, synchronous fluorescence spectroscopy, fourier transform infrared, and fluorescence resonance energy transfer in addition to molecular docking. Results from Stern Volmer equation stated that the quenching for MBZ-BSA binding was static. The fluorescence quenching spectroscopic study was performed at three temperature settings. The binding constant (kq), the number of binding sites (n), thermodynamic parameters (ΔHο, ΔSο and ΔGο), and binding forces were determined. The results exhibited that the interaction was endothermic. It was revealed that intermolecular hydrophobic forces led to the stabilization of the drug-protein system. Using the site marker technique, the binding between MBZ and BSA was found to be located at subdomain IIA (site I). This was furtherly approved using the molecular docking technique with the most stable MBZ configuration. This research may aid in understanding the pharmacokinetics and toxicity of MBZ and give fundamental data for its safe usage to avoid its toxicity.

Advancing Pyrrole Synthesis through DDQ Catalysis: A Comprehensive Research Incorporating DFT, ADMT, and Molecular Docking Analysis

“…As is generally recognized, BSA is an adequate model protein for study and comparison given its structural similarity to human serum albumin [69] . Gammal et al analyzed the interactions between mebendazole and BSA and recorded −6.9 kcal/mol binding affinity with the site I of subdomain IIA of BSA which is included in Arg194, Arg198, Ala290, Trp213, Arg217, Leu259, Leu237, Lys221, Ile289, Ile263, and Asp450 [70] . Wani et al recorded the interactions between indole derivative molecules and Ala212, Ala209, Leu454, Leu346, Leu480, Leu197, Val342, Val481, and Phe205 amino acids of BSA with −28.28kJ/mol binding affinity [71] .…”

“…[69] Gammal et al analyzed the interactions between mebendazole and BSA and recorded À 6.9 kcal/mol binding affinity with the site I of subdomain IIA of BSA which is included in Arg194, Arg198, Ala290, Trp213, Arg217, Leu259, Leu237, Lys221, Ile289, Ile263, and Asp450. [70] Wani et al recorded the interactions between indole derivative molecules and Ala212, Ala209, Leu454, Leu346, Leu480, Leu197, Val342, Val481, and Phe205 amino acids of BSA with À 28.28kJ/mol binding affinity. [71] In another study, possible anti-inflammatory pyrazoline pyridazine derivative molecules were analyzed against BSA by Al-Mehizia et al and they recorded one hydrogen bond Arg 194 and À 31.04 kJ/mol binding affinity.…”

Mixed ligand approach for novel hydrazide copper(II) complexes: Structural aspects, theoretical investigation and their biological evaluation

“…The value of n (number of the binding site) and K b (Binding constant) can be determined by utilizing Equation (). [ 66 ] …”

“…The value of n (number of the binding site) and K b (Binding constant) can be determined by utilizing Equation ( 2). [66] Log…”

A new fluorescence probe for sofosbuvir analysis in dosage form and spiked human plasma

“…Applying UV-visible absorption to explore reagent-drug interactions and ground state complex formation is a simple and readily accessible method [50,51,[55][56][57]. Differentiating between static and dynamic quenching is possible using UV-visible spectra.…”