Integrin α_Ⅱbβ₃ is a calcium-dependent heterodimeric protein on platelet, and its extracellular part can bind to RGD containing ligands. Here, a type of sensor prepared by transferring NTA-DOGS containing lipid monolayer to a 50 nm thick gold layer deposited on glass slide is reported. The surface binding ability and regeneration of the sensor were characterized by using a synthetic polypeptide P1 containing six histidine and RGD ligand. The specific binding of integrin to RGD ligand and the effect of divalent cations were investigated. The results show that His-tagged protein can be immobilized on the NTA sensor surface with a functional orientation and the results also show that removing of Ca²⁺ bound on low affinity sites or adding of Mn²⁺ can increase the binding ability of integrin.