Computational study for binding of oscillarin to human α-thrombin

Quantum mechanical calculation and molecular dynamics simulation have been carried out to study binding of Oscillarin (OSC), an antithrombotic marine natural product to human α-thrombin. The binding interaction energies between the inhibitor and individual protein fragments are calculated using a combination of HF and DFT methods. Study shows that the strong binding of OSC to Asp189, Ser214, Trp215, Gly216, and Gly219 is the primary mechanism of drug binding to thrombin. The individual residueligand interaction energies provide detailed quantitative information about specific residue interaction with the ligand that should be extremely useful to our understanding of the molecular nature of proteinligand binding.