Hollow-fiber capillary bundles are widely used in the production of medical devices for blood oxygenation and purification purposes such as in cardiopulmonary bypass, hemodialysis, and hemofiltration, but the blood interfacing inner surfaces of these capillaries provide poor hemocompatibility. Here, we present a novel method of packed-bed plasma ion implantation (PBPII) for the modification of the inner surfaces of polymeric hollow-fiber bundles enclosed in a cassette. The method is simple and can be performed on an intact hollow-fiber bundle cassette by the placement of a hollow cylindrical electrode, connected to a negative high-voltage pulse generator, around the cassette. The method does not require the insertion of electrodes inside the capillaries or the cassette. Nitrogen gas is fed into the capillaries inside the cassette by connecting the inlet of the cassette to a gas source. Upon the application of negative high-voltage bias pulses to the electrode, plasma is ignited inside the cassette, achieving the surface modification of both the internal and external surfaces of the capillaries. Fourier transform infrared-attenuated total reflectance spectroscopy of the PBPII-treated capillaries revealed the formation of aromatic C═C bonds, indicating the progressive carbonization of the capillary surfaces. The PBPII treatment was found to be uniform along the capillaries and independent of the radial position in the cassette. Atomic force microscopy of cross sections through the capillaries revealed that the increased stiffness associated with the carbonized layer on the inner surface of the PBPII-treated capillary has a depth (∼40 nm) consistent with that expected for ions accelerated by the applied bias voltage. The modified internal surfaces of the capillary bundle showed a greatly increased wettability and could be biofunctionalized by covalently immobilizing protein directly from the buffer solution. The direct, reagent-free protein immobilization was demonstrated using tropoelastin as an example protein. Covalent binding of the protein was confirmed by its resistance to removal by hot sodium dodecyl sulfate detergent washing, which is known to disrupt physical binding.

In our study, we monitored the inactivation of two important viruses that are critical in animal husbandry throughout the world. To evaluate the influence of the composting process on inactivation of avian influenza virus (H9N2) in poultry manure compost (PMC) and Encephalomyocarditis virus (EMCV) in pig (swine) manure compost (SMC), the H9N2 and EMCV were injected in dialysis cassettes and buried in two different manure compost piles of poultry and pig manure, respectively. The highest temperature achieved in the PMC and SMC piles during the test period were 75 °C and 73.5 °C, respectively. At the completion of the composting for 168 h, inactivation effect appeared to be more sensitive in H9N2 than EMCV. The vitality of H9N2 decreased by 6.25±0.35 log10TCID50/mL to 0.0 log10TCID50/mL within 1 h of the composting. The vitality of EMCV decreased from 7.75±0.35 log10TCID50/mL to 1.50 log10TCID50/mL within 24 h of starting the composting process. However, the activation of EMCV was not decreased (from 7.75±0.35 to 7.50±0.71 log10TCID50/mL) in the control treatment (not inserted in composts) after 168h, while the activation of H9N2 in dialysis cassettes was significantly decreased (from 6.25±0.35 log10TCID50/mL to 2.00±0.6 log10TCID50/mL). Our study demonstrated the effectiveness of the composting treatment in inactivating the viruses studied, which was not the case with air treatment.