Biophysical and structural characterization of tetramethrin serum protein complex and its toxicological implications

• DOI: 10.1002/jmr.3076
• Publication Date: 2024-02-17T08:35:11Z
• Authors: Pratik Singh; Priyanka Gopi; Majji Sai Sudha Rani; Shweta Singh; Prateek Pandya
• Keywords: Molecular mechanics; Human serum albumin; Docking (animal)

Abstract Tetramethrin (TMT) is a commonly used insecticide and has carcinogenic neurodegenerative effect on humans. The binding mechanism toxicological implications of TMT to human serum albumin (HSA) were examined in this study employing combination biophysical computational methods indicating moderate affinity potential hepato renal toxicity. Fluorescence quenching experiments showed that binds HSA with affinity, the process was spontaneous predominantly enthalpy‐driven. Circular dichroism spectroscopy revealed did not induce any significant conformational changes HSA, resulting no its alpha‐helix content. site modalities interactions as computed by molecular docking dynamics simulations it Sudlow II via hydrophobic through dimethylcyclopropane carboxylate methyl propanyl group. structural proper fit into creating increased stabilizing interactions. Additionally, mechanics–Poisson Boltzmann surface area calculations also indicated non‐polar van der Waals found be major contributors high free energy complex. Quantum mechanics (QM) energies confirmation degree deviation from global minimum conformation TMT. results provide comprehensive understanding which important for evaluating toxicity