Distinct Solute Removal Patterns by Similar Surface High-Flux Membranes in Haemodiafiltration: The Adsorption Point of View

<b><i>Introduction:</i></b> Haemodialysis (HD) allow depuration of uraemic toxins by diffusion, convection, and adsorption. Online haemodiafiltration (HDF) treatments add high convection to enhance removal. There are no prior studies on the relationship between convection and adsorption in HD membranes. The possible benefits conferred by intrinsic adsorption on protein-bound uraemic toxins (PBUTs) removal are unknown. <b><i>Methods:</i></b> Twenty-two patients underwent their second 3-days per week HD sessions with randomly selected haemodialysers (polysulfone, polymethylmethacrylate, cellulose triacetate, and polyamide copolymer) in high-flux HD and HDF. Blood samples were taken at the beginning and at the end of the treatment to assess the reduction ratio (RR) in a wide range of molecular weight uraemic toxins. A mid-range removal score (GRS) was also calculated. An elution protocol was implemented to quantify the amount of adsorbed mass (<i>M</i>_ads) for each molecule in every dialyser. <b><i>Results:</i></b> All synthetic membranes achieved higher RR for all toxins when used in HDF, specially the polysulfone haemodialyser, resulting in a GRS = 0.66 ± 0.06 (<i>p</i> &#x3c; 0.001 vs. cellulose triacetate and polyamide membranes). Adsorption was slightly enhanced by convection for all membranes. The polymethylmethacrylate membrane showed expected substantial adsorption of β₂-microglobulin (<i>M</i>_ads^HDF = 3.5 ± 2.1 mg vs. <i>M</i>_ads^HD = 2.1 ± 0.9 mg, <i>p</i> = 0.511), whereas total protein adsorption was pronounced in the cellulose triacetate membrane (<i>M</i>_ads^HDF = 427.2 ± 207.9 mg vs. <i>M</i>_ads^HD = 274.7 ± 138.3 mg, <i>p</i> = 0.586) without enhanced PBUT removal. <b><i>Discussion/Conclusion:</i></b> Convection improves removal and slightly increases adsorption. Adsorbed proteins do not lead to enhanced PBUTs depuration and limit membrane efficiency due to fouling. Selection of the correct membrane for convective therapies is mandatory to optimize removal efficiency.

Titanium and Protein Adsorption: An Overview of Mechanisms and Effects of Surface Features

Titanium and its alloys, specially Ti6Al4V, are among the most employed materials in orthopedic and dental implants. Cells response and osseointegration of implant devices are strongly dependent on the body–biomaterial interface zone. This interface is mainly defined by proteins: They adsorb immediately after implantation from blood and biological fluids, forming a layer on implant surfaces. Therefore, it is of utmost importance to understand which features of biomaterials surfaces influence formation of the protein layer and how to guide it. In this paper, relevant literature of the last 15 years about protein adsorption on titanium-based materials is reviewed. How the surface characteristics affect protein adsorption is investigated, aiming to provide an as comprehensive a picture as possible of adsorption mechanisms and type of chemical bonding with the surface, as well as of the characterization techniques effectively applied to model and real implant surfaces. Surface free energy, charge, microroughness, and hydroxylation degree have been found to be the main surface parameters to affect the amount of adsorbed proteins. On the other hand, the conformation of adsorbed proteins is mainly dictated by the protein structure, surface topography at the nano-scale, and exposed functional groups. Protein adsorption on titanium surfaces still needs further clarification, in particular concerning adsorption from complex protein solutions. In addition, characterization techniques to investigate and compare the different aspects of protein adsorption on different surfaces (in terms of roughness and chemistry) shall be developed.

Comparative Study of Oxidative Structural Modifications of Unadsorbed and Adsorbed Proteins in Whey Protein Isolate-Stabilized Oil-in-Water Emulsions under the Stress of Primary and Secondary Lipid Oxidation Products

The impact of typical primary or secondary lipid oxidation (LPO) products, selected as linoleic acid 13-hydroperoxide (13-HPODE) and malondialdehyde (MDA), on the structural modification of unadsorbed or adsorbed proteins in whey protein isolate (WPI)-stabilized oil-in-water (O/W) emulsions during storage up to 48 h at 37 °C in the dark was investigated. The results showed that either 13-HPODE and MDA could lead to structural modifications of unadsorbed or adsorbed proteins with a concentration-dependent manner and time relationship, respectively. Moreover, higher levels of MDA rendered a higher degree of oxidative modifications of WPI than 13-HPODE, indicated by the higher protein carbonyl contents and N’-formyl-L-kynurenine (NFK) and lower fluorescence intensity. Additionally, adsorbed proteins were more easily oxidized by LPO products than unadsorbed proteins. Overall, our results indicated that the formation of secondary LPO products and the protein position were crucial factors to increase the degree of oxidative modifications of WPI in O/W emulsion systems.

Protein Adsorption on SiO2-CaO Bioactive Glass Nanoparticles with Controllable Ca Content

Bioactive glass nanoparticles (BGNs) are emerging multifunctional building blocks for various biomedical applications. In this study, the primary aim was to develop monodispersed binary SiO2-CaO BGNs with controllable Ca content. We successfully synthesized such spherical BGNs (size ~110 nm) using a modified Stöber method. Our results showed that the incorporated Ca did not significantly affect particle size, specific surface area, and structure of BGNs. Concentrations of CaO in BGN compositions ranging from 0 to 10 mol% could be obtained without the gap between actual and nominal compositions. For this type of BGNs (specific surface area 30 m2/g), the maximum concentration of incorporated CaO appeared to be ~12 mol%. The influence of Ca content on protein adsorption was investigated using bovine serum albumin (BSA) and lysozyme as model proteins. The amount of adsorbed proteins increased over time at the early stage of adsorption (<2 h), regardless of glass composition and protein type. Further incubation of BGNs with protein-containing solutions seemed to induce a reduced amount of adsorbed proteins, which was more significant in BGNs with higher Ca content. The results indicate that the Ca content in BGNs is related to their protein adsorption behavior.

Correlation between Tribological Properties and the Quantified Structural Changes of Lysozyme on Poly (2-hydroxyethyl methacrylate) Contact Lens

The ocular discomfort is the leading cause of contact lens wear discontinuation. Although the tear proteins as a lubricant might improve contact lens adaptation, some in vitro studies suggested that the amount of adsorbed proteins could not simply explain the lubricating performance of adsorbed proteins. The purpose of this study was to quantify the structural changes and corresponding ocular lubricating properties of adsorbed protein on a conventional contact lens material, poly (2-hydroxyethyl methacrylate) (pHEMA). The adsorption behaviors of lysozyme on pHEMA were determined by the combined effects of protein–surface and protein–protein interactions. Lysozyme, the most abundant protein in tear, was first adsorbed onto the pHEMA surface under widely varying protein solution concentrations to saturate the surface, with the areal density of the adsorbed protein presenting different protein–protein effects within the layer. These values were correlated with the measured secondary structures, and corresponding friction coefficient of the adsorbed and protein covered lens surface, respectively. The decreased friction coefficient value was an indicator of the lubricated surfaces with improved adaptation. Our results indicate that the protein–protein effects help stabilize the structure of adsorbed lysozyme on pHEMA with the raised friction coefficient measured critical for the innovation of contact lens material designs with improved adaptation.

In Vitro Salivary Protein Adsorption Profile on Titanium and Ceramic Surfaces and the Corresponding Putative Immunological Implications

Immune responses triggered by implant abutment surfaces contributed by surface-adsorbed proteins are critical in clinical implant integration. How material surface-adsorbed proteins relate to host immune responses remain unclear. This study aimed to profile and address the immunological roles of surface-adsorbed salivary proteins on conventional implant abutment materials. Standardized polished bocks (5 × 5 × 1 mm3) were prepared from titanium and feldspathic ceramic. Salivary acquired pellicle formed in vitro was examined by liquid chromatography-tandem mass spectrometry and gene ontology (GO) analysis to identify and characterize the adsorbed proteins. Out of 759 proteins identified from pooled saliva samples, 396 were found to be attached to the two materials tested—369 on titanium and 298 on ceramic, with 281 common to both. GO annotation of immune processes was undertaken to form a protein–protein interaction network, and 14 hub proteins (≥6 interaction partners) (coding genes: B2M, C3, CLU, DEFA1, HSP90AA1, HSP90AB1, LTF, PIGR, PSMA2, RAC1, RAP1A, S100A8, S100A9, and SLP1) were identified as the key proteins connecting multiple (6–9) immune processes. The results offered putative immunological prospects of implant abutment material surface-adsorbed salivary proteins, which could potentially underpin the dynamic nature of implant–mucosal/implant–microbial interactions.