Structure of von Willebrand factor A1 on polystyrene determined from experimental and calculated sum frequency generation spectra.

ABSTRACT: The blood-clotting protein von Willebrand factor (vWF) can be activated by small molecules, high shear stress, and interactions with interfaces. It subsequently binds platelet receptor glycoprotein Ibα (GPIbα) at the surface of platelets, thereby playing a crucial role in blood clotting due to platelet activation, which is an important process to consider in the design of cardiovascular implants and biomaterials used in blood-contacting applications. The influence of surfaces on the activation and the molecular-level structure of surface-bound vWF is largely unknown. Recent studies have indicated that when bound to hydrophobic polystyrene (PS), the A1 domain of vWF remains accessible for GPIbα binding. However, the detailed secondary structure and exact orientation of vWF A1 at the PS surf

SUBMITTER: Roeters SJ 

PROVIDER: S-EPMC6294649 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature