Reduced bacterial adhesion to fibrinogen-coated substrates via nitric oxide release.

The ability of nitric oxide (NO)-releasing xerogels to reduce fibrinogen-mediated adhesion of Staphylococcus aureus, Staphylococcus epidermidis, and Escherichia coli is described. A negative correlation was observed between NO surface flux and bacterial adhesion for each species tested. For S.

Influence of glutathione and its derivatives on fibrin polymerization.

A complex relationship exists between reduced, oxidized, and nitrosated glutathione (GSH, GSSG, and GSNO, respectively). Although previous studies have demonstrated S-nitrosoglutathione (GSNO) has potent antiplatelet efficacy, little work has examined the role of GSNO and related species on subsequent aspects of coagulation (e.g.

Complexity of "A-a" knob-hole fibrin interaction revealed by atomic force spectroscopy.

During blood vessel injury, fibrinogen is converted to fibrin, a polymer that serves as the structural scaffold of a blood clot. The primary function of fibrin is to withstand the large shear forces in blood and provide mechanical stability to the clot, protecting the wound. Understanding the biophysical forces involved in maintaining fibrin structure is of great interest to the biomedical community.

Surface-dependent fibrinopeptide A accessibility to thrombin.

Fibrinogen adsorption and more recently fibrin formation at interfaces has been reported to depend on surface properties of the underlying substrate. To provide insight into the surface-dependent mechanism of fibrinopeptide A (FpA) release and fibrin formation, the accessibility and susceptibility of FpA to thrombin-catalyzed fibrinopeptide cleavage were examined using polyclonal anti-FpA IgG binding and surface plasmon resonance (SPR). The amount of accessible FpA on adsorbed fibrinogen was significantly influenced by surface properties of the underlying substrate (methyl- and carboxyl-terminated self-assembled monolayers).