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    Effect of Recombinant Human Perlecan Domain V Tethering Method on Protein Orientation and Blood Contacting Activity on Polyvinyl Chloride

    Year: 2021

    Journal: Adv. Healthc. Mater., Volume 10, JUL

    Authors: Chandrasekar, Keerthana; Farrugia, Brooke L.; Johnson, Lacey; Marks, Denese; Irving, David; Elgundi, Zehra; Lau, Kieran; Kim, Ha Na; Rnjak-Kovacina, Jelena; Bilek, Marcela M.; Whitelock, John M.; Lord, Megan S.

    Organizations: Australian Research Council [DP150104242, LP140101056, FL190100216]; Australian Government Research Training Program Scholarships; Heart Foundation of Australia Future Leader Fellowship [101896]; Research Infrastructure program at UNSW; Australian governments

    Keywords: blood; extracellular matrix; perlecan; plasma immersion ion implantation; platelets; polyvinyl chloride

    Surface modification of biomaterials is a promising approach to control biofunctionality while retaining the bulk biomaterial properties. Perlecan is the major proteoglycan in the vascular basement membrane that supports low levels of platelet adhesion but not activation. Thus, perlecan is a promising bioactive for blood-contacting applications. This study furthers the mechanistic understanding of platelet interactions with perlecan by establishing that platelets utilize domains III and V of the core protein for adhesion. Polyvinyl chloride (PVC) is functionalized with recombinant human perlecan domain V (rDV) to explore the effect of the tethering method on proteoglycan orientation and bioactivity. Tethering of rDV to PVC is achieved via either physisorption or covalent attachment via plasma immersion ion implantation (PIII) treatment. Both methods of rDV tethering reduce platelet adhesion and activation compared to the pristine PVC, however, the mechanisms are unique for each tethering method. Physisorption of rDV on PVC orientates the molecule to hinder access to the integrin-binding region, which inhibits platelet adhesion. In contrast, PIII treatment orientates rDV to allow access to the integrin-binding region, which is rendered antiadhesive to platelets via the glycosaminoglycan (GAG) chain. These effects demonstrate the potential of rDV biofunctionalization to modulate platelet interactions for blood contacting applications.
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