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Article Dans Une Revue Journal of Macromolecular Science Part B Physics Année : 2017

The Interaction of a New Schiff Base Ligand with Human Serum Albumin: Molecular Docking and Molecular Dynamics Simulation Studies

Iman Khosravi
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Mehdi Sahihi
Hadi Amiri Rudbari
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Ghazal Borhan
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Résumé

The interaction of a new heterocyclic Schiff base bearing pyridine and pyrimidine cycles, with human serum albumin (HSA) using molecular docking and molecular dynamics simulation methods was examined. Molecular docking studies showed that the ligand was bonded to the IB domain of the protein. It was found that there was one hydrogen bond interaction between HSA and the ligand. The standard Gibbs free energy for binding of the ligand to HSA was calculated as −9.63 kcal.mol−1. The results of the molecular dynamics simulation showed that the root mean square deviation (RMSD) of the non-liganded HSA and the HSA–ligand complex reached equilibration after 1000 ps. The study of the radius of gyration revealed that there was a conformational change when the HSA–ligand complex was formed. Finally, analyzing the RMS fluctuations (RMSF) suggested that the structure of the ligand binding site remained approximately rigid during the simulation.
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Dates et versions

hal-04086620 , version 1 (02-05-2023)

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Iman Khosravi, Mehdi Sahihi, Hadi Amiri Rudbari, Ghazal Borhan, Zahra Chavoshpour-Natanzi. The Interaction of a New Schiff Base Ligand with Human Serum Albumin: Molecular Docking and Molecular Dynamics Simulation Studies. Journal of Macromolecular Science Part B Physics, 2017, 56 (9), pp.636-643. ⟨10.1080/00222348.2017.1356634⟩. ⟨hal-04086620⟩
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