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Effect of Recombinant Human Perlecan Domain V Tethering Method on Protein Orientation and Blood Contacting Activity on Polyvinyl Chloride
Author(s) -
Chandrasekar Keerthana,
Farrugia Brooke L.,
Johnson Lacey,
Marks Denese,
Irving David,
Elgundi Zehra,
Lau Kieran,
Kim Ha Na,
RnjakKovacina Jelena,
Bilek Marcela M.,
Whitelock John M.,
Lord Megan S.
Publication year - 2021
Publication title -
advanced healthcare materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.288
H-Index - 90
eISSN - 2192-2659
pISSN - 2192-2640
DOI - 10.1002/adhm.202100388
Subject(s) - perlecan , chemistry , platelet activation , platelet , biophysics , glycosaminoglycan , adhesion , integrin , proteoglycan , biomaterial , microbiology and biotechnology , biochemistry , heparan sulfate , extracellular matrix , immunology , biology , organic chemistry , cell
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.