Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β(2)-glycoproteinI (β(2)-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β(2)-GPI binds to the negatively charged molecules, e.g. 7-ketochoresteryl-9-caboxynonanoate (oxLig-1) derived from the oxLDL and mediates the interaction between oxLDL and β(2)-GPI. In the present study, the oxLig-1/β(2)-GPI/anti-β(2)-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β(2)-GPI (rβ(2)-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β(2)-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ(2)-GPI DV significantly inhibits the formation of the oxLig-1/β(2)-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ(2)-GPI DV could be used to inhibit the formation of oxLDL/β(2)-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.