Comparison of the properties of phospholipid surfaces formed on HPA and L1biosensor chips for the binding of the coagulation factor VIII

Binding of a coagulation factor VIII to phosphatidylserine-containing membr anes is critical for exerting its cofactor activity. The use of surface pla smon resonance allows studying factor VIII interaction with immobilized pho spholipids. In the present study we compared factor VIII-binding properties of phospholipid surfaces immobilized on LI and HPA Biacore chips in the fo rm of a flexible bilayer and rigid monolayer, respectively. We demonstrated that immobilized phospholipid surfaces with physiological contents of PS a nd PE formed on L1 but not on HPA chip closely mimic intact phospholipid ve sicles in their factor VIII and thrombin-activated factor VIII (factor VIII a) binding properties. (C) 2001 Elsevier Science B.V. All rights reserved.