Journal Article

Unveiling Fluorescence Spectroscopy, Molecular Docking and Dynamic Simulations: Interactions Between Protein and 2, 4-Dinitrophenylhydrazine Schiff Base

Khan, Mohd S., Dash, Pragyan P., Rana, Tapan K., Barick, Aruna Kumar, Mishra, Swagatika, Mohapatra, Priyaranjan, Jali, Bigyan Ranjan, Tripathi, Sorav Sagar, Behera, Lingaraj, Mohanty, Patitapaban, Bhaskaran, R., Khan, Mohammad R., Jena, Pradip K.

2025

Overview

In this study, we aimed to explore the interaction mechanism between bovine serum albumin (BSA) and a Schiff base compound derived from 2,4-dinotrophenyl hydrazine ( L ) using various spectroscopic techniques. The interaction between BSA and synthesizing molecule can provide insights into binding affinity, conformational changes and potential applications in drug delivery or biochemistry. The interaction between BSA and L was studied by using UV-Vis and fluorescence titration analysis. The fluorescence quenching emission was observed at 343 nm, upon addition of L to the buffer solution of BSA. The binding between BSA and ligand is static in nature using fluorescence quenching emission. The thermodynamic parameters were calculated from the temperature-dependent binding constants (i.e., ∆H = -0.318 kcal/mol, ∆G = -7.857 kcal/mol and ∆S = 0.023 kcal/mol), which indicated that the protein-ligand complex formation between L and BSA is mainly due to the electrostatic interactions. The experimental and theoretical results showed excellent agreement with respect to the mechanism of binding and binding constants. The molecular docking and molecular dynamic analysis experiments were performed to establish the interaction between protein and ligand.

• Publisher: Springer US,Springer Nature B.V
• Subject: Analytical Chemistry / Animals / Binding / Bioavailability / Biochemistry / Biological and Medical Physics / Biomedical and Life Sciences / Biomedical research / Biomedicine / Biophysics / Biotechnology / Bovine serum albumin / Buffer solutions / Cattle / Chemical synthesis / Chemistry / Complex formation / Drug delivery / Drug delivery systems / Drugs / Electrostatic properties / Emission / Fluorescence / Fluorescence spectroscopy / Hydrazine / Hydrazines / Imines / Ligands / Medical research / Molecular docking / Molecular Docking Simulation / Molecular dynamics / Molecular Dynamics Simulation / Molecular weight / Permeability / Pharmaceutical industry / Pharmacokinetics / Phenylhydrazines - chemistry / Phenylhydrazines - metabolism / Protein Binding / Proteins / Protons / Quenching / Schiff Bases - chemistry / Schiff Bases - metabolism / Serum albumin / Serum Albumin, Bovine - chemistry / Serum Albumin, Bovine - metabolism / Spectrometry, Fluorescence / Temperature dependence / Thermodynamics / Titration