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New surface coatings that enhance hemocompatibility and biofunctionality of synthetic vascular grafts such as expanded poly(tetrafluoroethylene) (ePTFE) and poly(ethylene terephthalate) (PET) are urgently needed. Lubricant-infused surfaces prevent nontargeted adhesion and enhance the biocompatibility of blood-contacting surfaces. However, limited success has been made in incorporating biofunctionality onto these surfaces and generating biofunctional lubricant-infused coatings that both prevent nonspecific adhesion and enhance targeted binding of biomolecules remains a challenge. Here, a new generation of fluorosilanized lubricant-infused PET surfaces with built-in biofunctional nanoprobes is reported. These surfaces are synthesized by starting with a self-assembled monolayer of fluorosilane that is partially etched using plasma modification technique, thereby creating a hydroxyl-terminated fluorosilanized PET surface. Simultaneously, silanized nanoprobes are produced by amino-silanizing anti-CD34 antibody in solution and directly coupling the anti-CD34-aminosilane nanoprobes onto the hydroxyl terminated, fluorosilanized PET surface. The PET surfaces are then lubricated, creating fluorosilanized biofunctional lubricant-infused PET substrates. Compared with unmodified PET surfaces, the designed biofunctional lubricant-infused PET surfaces significantly attenuate thrombin generation and blood clot formation and promote targeted binding of endothelial cells from human whole blood.

The new oral anticoagulants are rapidly replacing warfarin for several indications. In contrast to warfarin, which lowers the functional levels of all of the vitamin K-dependent clotting factors, the new agents target either factor Xa or thrombin. With targeted inhibition of coagulation, the new oral anticoagulants have pharmacological, biochemical, and clinical features distinct from those of warfarin. Focusing on laboratory perspectives, this article compares and contrasts the pharmacological and biochemical properties of the new oral anticoagulants with those of warfarin and uses this information to speculate on the underlying mechanisms responsible for the clinical features that differentiate the new agents from warfarin.

The limitations of traditional anticoagulants, heparin and warfarin, have prompted the development of new anticoagulant drugs for prevention and treatment of both venous and arterial thromboembolism. After a brief review of thrombogenesis and its regulation, this paper focuses on new anticoagulant agents in more advanced stages of clinical testing.

Summary An asymptomatic 50-year-old male with a gamma globulin paraprotein was found to have prolonged prothrombin time, activated partial thromboplastin time, and thrombin time but a normal reptilase time. The prolonged clotting times were not the result of a factor deficiency because they were not corrected by the addition of normal plasma. Instead, this patient had an antibody that delayed thrombin-mediated fibrinopeptide B release thereby producing an apparent dysfibrinogenaemia. His isolated IgG prolonged the thrombin clotting time of both normal plasma and fibrinogen. Precincubation of his IgG with fibrinopeptide B, but not with fibrinopeptide A or thrombin, decreased its ability to prolong the thrombin clotting time. The patient's purified IgG but not control IgG delayed thrombin-mediated fibrinopeptide B release from fibrinogen without affecting the release of fibrinopeptide A. These studies define a novel, clinically silent dysfibrinogenaemia due to an antibody that delays thrombin-mediated fibrinopeptide B release from fibrinogen thereby markedly prolonging the clotting times.