An insight into the interaction between malachite green oxalate with human serum albumin: Molecular dynamic simulation and spectroscopic approaches
| Autor: | Masoumeh Kooravand, Saeid Asadpour, Hedayat Haddadi, Sadegh Farhadian |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Environmental Engineering
Molecular model Health Toxicology and Mutagenesis 0211 other engineering and technologies Environmental pollution Serum Albumin Human 02 engineering and technology 010501 environmental sciences Molecular Dynamics Simulation 01 natural sciences chemistry.chemical_compound Molecular dynamics Computational chemistry medicine Rosaniline Dyes Environmental Chemistry Humans Malachite green Waste Management and Disposal Serum Albumin 0105 earth and related environmental sciences chemistry.chemical_classification 021110 strategic defence & security studies Oxalates Binding Sites Biomolecule Circular Dichroism Cationic polymerization Human serum albumin Pollution body regions Molecular Docking Simulation Spectrometry Fluorescence chemistry Docking (molecular) embryonic structures Thermodynamics medicine.drug Protein Binding |
| Zdroj: | Journal of hazardous materials. 407 |
| ISSN: | 1873-3336 |
| Popis: | Cationic triarylmethane dyes such as malachite green are aromatic xenobiotic compounds causing environmental pollution. The affinity between hazardous materials and biomolecules makes it important to understand the properties of such compounds. Accordingly, in this study, the possible molecular interaction between this pollutant and the human serum albumin (HSA) was investigated using a combination of molecular docking, molecular dynamic simulation and multi-spectroscopic approaches. The docking results illustrated that malachite green oxalate (MGO) could bind to some of the HSA amino acids with the estimated free energy = −32.93 kJ/mol. Further, the results of the dynamic simulation revealed that MGO had a steady interaction with the protein though increasing flexibility and decreasing the HSA compactness. These results were, therefore, in agreement with those obtained by spectroscopic techniques. The MGO concentration of 0.0005 mM could quench the HSA’s intrinsic fluorescence by %16.88. The protein structural changes also revealed that the binding interaction of MGO-HSA was accompanied by an increase in the α-helix and a decrease in the β-sheet of the protein. Overall, this study indicated the suitable molecular modeling interaction of MGO and HSA. |
| Databáze: | OpenAIRE |
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