The GROMACS software, employing the amber ff14sb force field, was utilized to conduct molecular dynamics simulations on both proteins and protein-ligand complexes. To maintain stability, the SETTLE algorithm was employed for water molecule bond lengths and angles, while the LINCS algorithm was applied to constrain the bond lengths of protein. Long-range electrostatic interactions were computed using the particle-mesh Ewald (PME) method. The protein-ligand complex was placed in the box of dimensions 1 Å form the surface of the protein and was filled with TIP3P water molecules. Sodium (Na+) and chloride (Cl-) ions were introduced to uphold physiological ion levels. Energy minimization comprised 5000 steps, followed by equilibration steps (nvt and npt) each lasting 1000 steps. The ensuing molecular dynamics simulations persisted for 500 ns, employing 2 fs time steps and maintaining constant particle count, pressure, and temperature (NPT ensemble). Representative structures were gleaned via cluster analysis. Binding energies between host and guest molecules were evaluated using the molecular mechanics/Poisson-Boltzmann surface area (MMGBSA) method.