von Willebrand Factor (VWF) is a soluble blood clotting protein.  Previous studies in our lab have shown surface characteristics influence adsorbed structure and function of the platelet binding domain of VWF (A1 domain).   Structural changes are also important in clinical VWF mutants.  Here, we use surface analysis techniques to obtain greater detail about structural differences of VWF adsorbed onto different surfaces. Near-edge x-ray absorption fine structure was used to identify differences in the amide backbone of A1 adsorbed to polystyrene, tissue culture polystyrene, and glass.  Differences in the sum frequency generation amide spectra also suggested structural differences in adsorbed A1 on different surfaces.  Time-of-flight secondary ion mass spectrometry data showed differences between clinical A1 mutants when adsorbed to different surfaces, as well as differences between the proteins when adsorbed to the same surface, suggesting conformational changes induced by surface adsorption may be different from changes caused by mutation.

Structure and function analysis of surface-immobilized wildtype von Willebrand Factor and clinical von Willebrand Factor mutants

243rd National Meeting (2012)

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