Interaction Studies of a Novel Enantiopure Isoxazolidine with DNA and β-Cyclodextrin: Binding and Antioxidant Properties | ||
| Egyptian Journal of Chemistry | ||
| Articles in Press, Accepted Manuscript, Available Online from 20 October 2025 | ||
| Document Type: Original Article | ||
| DOI: 10.21608/ejchem.2025.415613.12218 | ||
| Authors | ||
| Kaiss Aouadi* 1; Etab AlRashidi2 | ||
| 1Department of Chemistry, College of Science, Qassim University | ||
| 2Department of Chemistry, College of Science, Qassim University, Buraidah 51452, Saudi Arabia | ||
| Abstract | ||
| Using UV-Vis and fluorescence spectroscopy, this work examines how ISoXD4 interacts with DNA and β-cyclodextrin (β-CD). Intercalation was indicated by a red shift (307 nm to 320 nm) and a hypochromic impact in ISoXD4 absorption upon DNA binding, as shown by UV-Vis analysis. With ΔG° = -20.78 kJ·mol⁻¹ and a binding constant (Kb) of 4.37 × 10³ M⁻¹, spontaneous binding was confirmed. Dynamic interaction was supported by fluorescence tests that revealed an initial emission enhancement followed by quenching at increasing DNA concentrations. ISoXD4 displaces ethidium bromide (EB), according to competitive experiments using EB; static quenching was indicated by Ksv = 4.15 × 10³ M⁻¹ and kq = 2.08 × 10¹¹ M⁻¹ s⁻¹. There was a 1:1 stoichiometry, and the binding site value (n) was equal to 0.994. UV-Vis revealed a hypsochromic shift for β-CD (308 nm to 300 nm), indicating that ISoXD4 is encapsulated in the hydrophobic cavity. ΔG° = -11.07 kJ·mol⁻¹ and Kb = 87.0 M⁻¹ suggested the production of a spontaneous compound. Fluorescence tests showed a 33% increase in emission intensity at 390 nm, indicating successful encapsulation within the β-CD cavity. The binding site value (n) of 0.606 suggests a 2:1 (β-CD : ISoXD4) stoichiometry for the inclusion complex, revealing a specific host-guest interaction mode. ISoXD4 was investigated for its antioxidant potential through DPPH assay, and ABTS radical scavenging assays having IC50 17.85±0.51 μM and 15.83±0.3 μM, respectively. Furthermore, molecular docking analysis revealed that the interaction mode of ISoXD4 against cytochrome c peroxidase protein (PDB code: 2X08) involved π-π stacking, hydrophobic interactions and extensive van der Waals interactions. Molecular dynamics (MD) simulation indicates that ISoXD4 remains stably bound within the peroxidase enzyme’s active site. Molecular dynamics (MD) simulations demonstrate that ISoXD4 maintains a stable binding within the active site of the peroxidase enzyme. | ||
| Keywords | ||
| DNA; β-cyclodextrin; isoxazolidine; antioxidants; UV-Vis absorption | ||
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