Molecular docking were used to investigate the interaction of Sunitinib with VEGFR-2. A 10 ns molecular dynamics (MD) calculation was performed to study the complex and the results indicate that Sunitinib can produce hydrophobic interactions with the nonpolar side chains of the residues (Glu885, Ile888, His1026, Asp1028, Asp1046) in the binding pocket. Moreover, the three residues (His1026, Cys1024, Asp1046) ground Sunitinib can form H-bonds with Sunitinib, which can produce significant contribution to biological activities. The result of our simulation will provide theoretical basis for molecular structure improvement, molecular design, molecular synthesis of VEGFR-2 inhibitor, and will be useful in finding higher activity, better anticancer drugs.

Key words: VEGFR-2, Sunitinib, molecular docking, molecular dynamics