Integrated quantum chemical and molecular dynamics studies of isoscopoletin against Mycobacterium tuberculosis thymidylate kinase

and a bioavailability score of 0.55. Molecular docking suggested strong binding affinity, which was further validated by 200 ns molecular dynamics simulations. The protein-ligand complex exhibited stable RMSD values ranging from 1.0 to 2.6 Å (average ≈ 1.8 Å) compared to the free protein (1.8-3.0 Å; average ≈ 2.4 Å), indicating enhanced stability upon ligand binding. RMSF analysis showed minimal residue fluctuations (0.05-0.20 nm), while the radius of gyration remained stable between 1.60 and 1.72 nm. Principal component analysis revealed that the first three components (PC1: 26.16%, PC2: 14.45%, PC3: 9.14%) accounted for 49.8% of the total motion, indicating coordinated and stable dynamics. These computational findings demonstrate that isoscopoletin exhibits favorable electronic properties, stable protein-ligand interactions, and good pharmacokinetic characteristics, supporting its application as an anti-tubercular drug.