Surface gradient of functional heparin

David E. Robinson, Andrew Marson, Robert D. Short, David J. Buttle, Anthony J. Day, Kristina L. Parry, Michelle Wiles, Peter Highfield, Anita Mistry, Jason D. Whittle

    Research output: Contribution to journalArticlepeer-review


    A simple method for forming a functional gradient of unmodified heparin by adsorption onto a surface chemical gradient was reported to find effects of surface chemistry on the binding of heparin. It is seen that there is a significant increase in S content along the length of the gradient, starting at 0.25 at the octadiene end of the gradient and rising to 0.62 at the allyl amine end. The binding of Link_TSG6 increases across the gradient, while over the mid-portion of the gradient, the amount of bound heparin and bound protein increase in an equivalent manner. The functionality of the surface-bound heparin is found to be optimal when adsorbed to plasma-polymerized allyl amine surfaces with an N/C ratio of 0.15. Optimal protein binding is found to require a specific level of surface adsorption, which if exceeded, leads to heparin immobilized in a less functional form.
    Original languageEnglish
    Pages (from-to)1166-1169
    Number of pages3
    JournalAdvanced Materials
    Issue number6
    Publication statusPublished - 18 Mar 2008


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