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<p>In this study, the anticancer drug PD128763 was evaluated for its interaction with graphene oxide as a nanocarrier and with the Poly(ADP-ribose) Polymerase (PARP) protein (PDB ID: 5HA9), using computational approaches. Density functional theory (DFT) calculations revealed favorable adsorption energies, indicating the thermodynamic stability of the drug-carrier complex. Quantum theory of atoms in molecules (QTAIM) analyses confirmed noncovalent interactions along with significant hydrogen bonds. UV-Vis spectra exhibited shifts due to charge transfer and electronic polarization effects. Solvent studies showed enhanced stability in polar media. Molecular docking of PD128763 with PARP revealed strong binding affinity and interactions with key active site residues. Subsequently, a 130 ns molecular dynamics (MD) simulation of the drug-protein complex was performed. The results confirmed the structural stability and strong interactions within the binding site. These findings suggest that PD128763 exhibits stable and effective binding both on the graphene oxide surface and with its biological target, proposing it as a suitable candidate for targeted anticancer drug delivery.</p>

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Computational design of graphene oxide-based delivery of PD128763 PARP inhibitor: DFT, molecular dynamics, and molecular docking analysis

  • 期刊论文

  • 发表日期：

    2025年12月10日

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  • Fahime Alikhoshi,
  • Mehdi Sadeghi,
  • Ali Arab

摘要

In this study, the anticancer drug PD128763 was evaluated for its interaction with graphene oxide as a nanocarrier and with the Poly(ADP-ribose) Polymerase (PARP) protein (PDB ID: 5HA9), using computational approaches. Density functional theory (DFT) calculations revealed favorable adsorption energies, indicating the thermodynamic stability of the drug-carrier complex. Quantum theory of atoms in molecules (QTAIM) analyses confirmed noncovalent interactions along with significant hydrogen bonds. UV-Vis spectra exhibited shifts due to charge transfer and electronic polarization effects. Solvent studies showed enhanced stability in polar media. Molecular docking of PD128763 with PARP revealed strong binding affinity and interactions with key active site residues. Subsequently, a 130 ns molecular dynamics (MD) simulation of the drug-protein complex was performed. The results confirmed the structural stability and strong interactions within the binding site. These findings suggest that PD128763 exhibits stable and effective binding both on the graphene oxide surface and with its biological target, proposing it as a suitable candidate for targeted anticancer drug delivery.