Abstract
The correlation between the interfacial structure and protein adsorption at a polymer/water interface was investigated. Poly(2-methoxyethyl acrylate)(PMEA), which is one of the best blood compatible polymers available, was employed. Nanometer-scale structures generated through the phase separation of polymer and water were observed at the PMEA/phosphate buffered saline interface. The interaction between the interfacial structures and fibrinogen (FNG) was measured using atomic force microscopy. Attraction was observed in the polymer-rich domains as well as in the non-blood compatible polymer. In contrast, no attractive interactions were observed, and only a repulsion occurred in the water-rich domains. The non-adsorption of FNG into the water rich domains was also clarified through topographic and phase image analyses. Furthermore, the FNG molecules adsorbed on the surface of PMEA were easily desorbed, even in the polymer-rich domains. Water molecules in the water-rich domains are anticipated to be the dominant factor in preventing FNG adsorption and thrombogenesis on a PMEA interface.
Highlights
When blood comes into contact with a foreign material, various biological defense systems, such as the complement, blood coagulation, and inflammation systems are promptly activated (Gorbet et al, 2004; Anderson et al, 2008; Sperling et al, 2009; Arima et al, 2010)
For the Poly(2-methoxyethyl acrylate) (PMEA), the amount of adsorbed FNG is suppressed more than the amounts of PP and poly(butyl acrylate) (PBA)
It is thought that no suppression of FNG adsorption occurred and that the aggregation among the proteins enhanced the degeneration on the PBA
Summary
When blood comes into contact with a foreign material, various biological defense systems, such as the complement, blood coagulation, and inflammation systems are promptly activated (Gorbet et al, 2004; Anderson et al, 2008; Sperling et al, 2009; Arima et al, 2010) Medical devices such as artificial blood vessels, catheters, and stents require high antithrombogenicity to suppress thrombus formation on the material surface. These biological reactions are triggered by the adsorption of proteins on the material surface in a biological environment (Chen et al, 2008).
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