Abstract
Studies on the interactions of tissue plasminogen activator (tPA) and plasminogen with polyurethane surfaces containing ฯตโlysine moieties (ฯตโamino group free) are reported. These surfaces are considered to have the potential to dissolve nascent clots that may be formed on them. For adsorption from both single protein solutions and plasma, the surfaces were found to have a high capacity for tPA as well as plasminogen. A significant fraction of preadsorbed tPA was displaced from the ฯตโlysine surfaces upon contact with plasma. These surfaces, when preadsorbed with tPA and then incubated with plasma, were able to dissolve incipient clots formed around them. However, the clotโdissolving capacity diminished as the time of plasma incubation increased, presumably due to loss of tPA. It was also shown that in plasma, preadsorbed tPA is displaced from these surfaces largely by plasminogen, which thus appears to have a greater binding affinity than tPA for the ฯตโlysine moieties. Finally, it was found that in plasma, the ฯตโlysine surfaces interact with plasminogen in a dynamic manner, and that about 70% of the bound plasminogen is exchanging continuously with plasminogen in the plasma. ยฉ 2003 Wiley Periodicals, Inc. J Biomed Mater Res 66A: 795โ801, 2003