Protein adsorption on polyurethane catheters modified with a novel antithrombin-heparin covalent complex

Highly anticoagulant covalent antithrombin‐heparin complex (ATH) was covalently grafted onto polyurethane catheters to suppress adsorption/activation of procoagulant proteins and enhance adsorption/activation of anticoagulant proteins for blood compatibility. Consistency of catheter coating was demo...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biomedical materials research. Part A 2007-01, Vol.80A (1), p.216-225
Main Authors: Du, Ying Jun, Brash, John L., McClung, Glen, Berry, Leslie R., Klement, Petr, Chan, Anthony K.C.
Format: Article
Language:English
Subjects:
Adsorption
Animals
anticoagulant
antithrombin
Antithrombins
Blood Coagulation
Catheterization
Coated Materials, Biocompatible - chemistry
Factor Xa - chemistry
Factor Xa Inhibitors
Fibrinogen - chemistry
heparin
Heparin - chemistry
Materials Testing
polyurethane
Polyurethanes - chemistry
Protein Binding
Rabbits
Serum Albumin - chemistry
surface grafting
Surface Properties
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Highly anticoagulant covalent antithrombin‐heparin complex (ATH) was covalently grafted onto polyurethane catheters to suppress adsorption/activation of procoagulant proteins and enhance adsorption/activation of anticoagulant proteins for blood compatibility. Consistency of catheter coating was demonstrated using immunohistochemical visualization of ATH. The ability of the resulting immobilized ATH heparin chains to bind antithrombin (AT) from plasma, as measured by binding of 125I‐radiolabeled AT, was greater than that for commercially‐available heparin‐coated catheters, and much greater than for uncoated catheters. Complementary measurements of antifactor Xa (FXa) activity and plasma protein binding were also performed. Both ATH‐coated and heparin‐coated catheters demonstrated functional binding of exogenous AT. However, the ATH‐coated catheters gave a trend towards elevated anti‐ FXa activities/AT binding ratios, consistent with the higher active pentasaccharide content in starting ATH. Western blot analysis of proteins adsorbed to catheters after incubation with rabbit plasma established protein binding profiles that showed AT and albumin as major plasma proteins adsorbed to ATH‐coated catheters, while AT and altered forms of fibrinogen were major plasma protein species adsorbed to heparinized catheters. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2007
ISSN:1549-3296
1552-4965
DOI:10.1002/jbm.a.30977