Electrostatic Repulsive Features of Free-Standing Titanium Dioxide Nanotube-Based Membranes in Biofiltration Applications.

This study presents the electrostatic repulsive features of electrochemically fabricated titanium dioxide nanotube (NT)-based membranes with different surface nanomorphologies in cross-flow biofiltration applications while maintaining a creatinine clearance above 90%. Although membranes exhibit antifouling behavior, their blood protein rejection can still be improved. Due to the electrostatically negative charge of the hexafluorotitanate moiety, the fabricated biocompatible, superhydrophilic, free-standing, and amorphous ceramic nanomembranes showed that about 20% of negatively charged 66 kDa blood albumin was rejected by the membrane with ∼100 nm pores. As the nanomorphology of the membrane was shifted from NTs to nanowires by varying fabrication parameters, pure water flux and bovine serum albumin (BSA) rejection performance were reduced, and the membrane did not lose its antifouling behavior. Herein, nanomembranes with different surface nanomorphologies were fabricated by a multi-step anodic oxidation process and characterized by scanning electron microscopy, atomic force microscopy, water contact angle analysis, X-ray diffraction, and energy-dispersive X-ray spectroscopy. The membrane performance of samples was measured in 3D printed polyethylene terephthalate glycol flow cells replicating implantable artificial kidney models to determine their blood toxin removal and protein loss features. In collected urine mimicking samples, creatinine clearances and BSA rejections were measured by the spectrophotometric Jaffe method and high-performance liquid chromatography.

Adsorption behavior of serum proteins on anodized titanium is driven by surface nanomorphology.

Protein adsorption behavior can play a critical role in defining the outcome of a material by affecting the subsequent in vivo response to it. To date, the effect of surface properties on protein adsorption behavior has been mainly focused on surface chemistry, but research on the effect of nanoscale surface topography remains limited. In this study, the adsorption behavior of human serum albumin, immunoglobulin G, and fibrinogen in terms of the adsorbed amount and conformational changes were investigated on bare and anodized titanium (Ti) samples (40 and 60 V applied voltages). While the surface chemistry, RMS surface roughness, and arithmetic surface roughness of the anodized samples were similar, they had distinctly different nanomorphologies identified by atomic force microscopy and scanning electron microscopy, and the surface statistical parameters, surface skewness Ssk and kurtosis Sku. The Feret pore size distribution was more uniform on the 60 V sample, and surface nanostructures were more symmetrical with higher peaks and deeper pores. On the other hand, the 40 V sample surface presented a nonuniform pore size distribution and asymmetrical surface nanostructures with lower peaks and shallower pores. The amount of surface-adsorbed protein increased on the sample surfaces in the order of Ti < 40 V < 60 V with the predominant factor affecting the amount of surface-adsorbed protein being the increased surface area attained by pore formation. The secondary structure of all adsorbed proteins deviated from that of their native counterparts. While comparing the secondary structure components of proteins on anodized surfaces, it was observed that all three proteins retained more of their secondary structure composition on the surface with more uniform and symmetrical nanofeatures than the surface having asymmetrical nanostructures. Our results suggest that the nanomorphology of the peaks and outer walls of the nanotubes can significantly influence the conformation of adsorbed serum proteins, even for surfaces having similar roughness values.