Structural investigations of VWF under flow by FTIR spectroscopy

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This proposal aims at the FTIR spectroscopic analysis of Von Willebrand Factor (vWF) structural plasticity under induced and controlled shear flow. vWF is the mechanosensoric protein which triggers primary hemostasis. The approach is based on the multidisciplinary design of a surface acoustic wave (SAW) driven flow cell device. This will enable the in detail structural analysis of vWF in a most native environment. Both polymeric full length, multidomain vWF complexes and single, functional domains will be analyzed. At least one surface of the flow device will be functionalizable. Thus, a specific immobilization of a vWF domain or a binding partner within adjustable shear flow will be used for binding studies. Further analysis of the enzymatic vWF cleavage with ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13) will give structural information about hemostasis regulation.