Adsorption Of Bovine Serum Albumin Research Articles

Thermo- and pH-Responsible Gels for Efficient Protein Adsorption and Desorption

Protein adsorption behavior was examined on poly(N-isopropylacrylamide-co-sodium methacrylate)-based hydrogels at different temperatures: 5, 20, and 37 °C, and pH: 4.5, 7, and 9.2. The hydrogels, whose covalent skeleton contains pendant anionic units due to the presence of the sodium methacrylate co-monomer, exhibited both thermo- and pH-sensitivity with different extents, which depended on the content of ionizable moieties and the cross-linker density. The hydrogel composition, temperature, and pH influenced the zeta potential of the hydrogels and their swelling properties. The proteins selected for the study, i.e., bovine serum albumin (BSA), ovalbumin (OVA), lysozyme (LYZ), and a monoclonal antibody (mAb2), differed in their aminoacidic composition and conformation, thus in isoelectric point, molecular weight, electrostatic charge, and hydrophobicity. Therefore, the response of their adsorption behavior to changes in the solution properties and the hydrogel composition was different. LYZ exhibited the strongest adsorption of all proteins with a maximum at pH 7 (189.5 mg ggel−1); adsorption of BSA and OVA reached maximum at pH 4.5 (24.4 and 23.5 mg ggel−1), whereas mAb2 was strongly adsorbed at 9.2 (21.7 mg ggel−1). This indicated the possibility of using the hydrogels for pH-mediated separation of proteins differing in charge under mild conditions in a water-rich environment of both the liquid solution and the adsorbed phase. The adsorption affinity of all proteins increased with temperature, which was attributed to the synergistic effects of attractive electrostatic and hydrophobic interactions. That effect was particularly marked for mAb2, for which the temperature change from 5 to 37 °C caused a twentyfold increase in adsorption. In all cases, the proteins could be released from the hydrogel surface by a reduction in temperature, an increase in pH, or a combination of both. This allows for the elimination of the use of salt solution as a desorbing agent, whose presence renders the recycling of buffering solutions difficult.

Investigations on the complexation and binding mechanism of bovine serum albumin with Ag-doped TiO2 nanoparticles.

It is essential to study the interactions between nanoparticles and proteins to better understand the biological interactions of nanoparticles. In this study, we studied the protein adsorption mode on the surface of Ag-doped TiO2 nanoparticles (NPs) using a model protein, bovine serum albumin (BSA). The mechanism of binding BSA to the Ag-doped TiO2 NPs was studied by applying fluorescence quenching, absorbance measurements, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy techniques. The strong binding between BSA and Ag-doped TiO2 NPs was confirmed by a high value of binding constant (K = 2.65 × 105 L mol-1). We also studied the thermal stability of BSA in the presence of the Ag-doped TiO2 NPs. Thermodynamic parameters indicated that the adsorption of BSA on the Ag-doped TiO2 NPs was a spontaneous, natural and exothermic process. The effect of Ag-doped TiO2 NPs on the transportation function of BSA was also studied using a fluorescence spectroscopic technique. Fluorescence spectroscopic data suggested the existence of a strong interaction between BSA and the surface of the Ag-doped TiO2 NPs, which indicated that the binding affinities of some selected amino acids in BSA changed. This, in turn, clearly confirms that the Ag-doped TiO2 NPs affect the transportation capability of BSA in blood.

Optimizing PES microfiltration membranes for sterile filtration: A comparative study of polydopamine coating in acidic and basic conditions to minimize protein adsorption

The increasing need for effective sterile filtration in the pharmaceutical industry calls for advancements in microfiltration (MF) membrane technology that can effectively reduce fouling and preserve essential protein products. Our study highlights the crucial role of improving the hydrophilicity throughout the entire membrane, not just on the surface, to decrease both protein adsorption and fouling. We have developed a facile but effective method for producing hydrophilic porous polyethersulfone (PES) MF membranes using vapor-induced phase separation (VIPS) followed by a hydrophilic coating. By meticulously adjusting the vapor exposure time, we fabricated two specific types of symmetric membranes: a standard one with a mean pore size of 0.22 μm and another designed with slightly larger pores for the subsequent polydopamine (PDA) coating. All membranes developed in this study showed an outstanding sterilization performance (over 99.99999 % bacteria rejection) due to the absence of defects. Our comparative studies of PDA coating in both acidic and basic environments revealed that the PDA-modified membranes in a Tris-HCl buffer (pH 8.0) (PDA-b-PES2M) outperform others in performance of protein microfiltration. While the membrane modified under acidic conditions underwent a gradual degradation of PDA leading to a poor filtration performance, the PDA-b-PES2M membranes showcased remarkable anti-fouling properties, greatly minimizing the adsorption of bovine serum albumin (BSA) and simplifying the removal of adsorbed materials. Our optimized membrane has a great potential for sterile filtration applications where minimizing protein loss is crucial.

Adsorption and Morphology Analysis of Bovine Serum Albumin on a Micropillar-Enhanced Quartz Crystal Microbalance.

The adsorption of bovine serum albumin (BSA), a widely used blood plasma protein, onto poly(methyl methacrylate) (PMMA) surface is a fundamental phenomenon attracting increasing interests in molecular biology, cell culture, immunology, diagnostics, and vaccinology. The nanostructured PMMA surfaces have shown a considerable effect on the BSA adsorption process. However, the effect of microstructures (e.g., micropillars) on BSA adsorption has seldom been studied. This research reports on the development of an acoustic resonance based method to explore the adsorption of BSA proteins on PMMA micropillars in terms of surface coverage, apparent binding constants, and pH-induced morphology variation. A theoretical model is developed to understand the frequency changes of QCM induced by BSA adsorption by taking into consideration the effects of the hydrodynamic force and an equivalent BSA/liquid layer formed on the micropillar surface. In addition, it was found that the resonance of micropillars with a quartz crystal microbalance (QCM) substrate significantly influenced BSA adsorption on micropillar surfaces.

A readily accessible quaternized cellulose filter paper with high permeability for IgG separation

Anion-exchange chromatography (AEC) is recognized as a highly effective approach for the purification of immunoglobulin G (IgG). This study introduces an innovative strategy that employs waste cellulose filter paper in the production of AEC media. A quaternized cellulose fiber membrane (CFM-QCS) was successfully fabricated that cellulose fibers were as a structural framework, glutaraldehyde (GA) as a crosslinking agent, and quaternary chitosan (QCS) as a modifying agent. Morphological and chemical characterization revealed that GA and QCS were uniformly crosslinked on the surface of the cellulose fibers, resulting in excellent mechanical properties in both dry and wet states. Benefiting from its 3D network scaffold structure, CFM-QCS demonstrated a high adsorption capacity for bovine serum albumin (BSA), with static and dynamic adsorption capacities of 605.15 mg/g and 88.63 mg/ml, respectively. After treated with extreme conditions and 10 cyclic adsorption and elution, the adsorption capacity of CFM-QCS remains almost unchanged, highlighting its excellent stability. Additionally, a CFM-QCS packed chromatography column exhibited high flux of 10.38 L/h at 0.1 MPa, which can efficiently separate IgG from a mixed solution in the presence of BSA and IgG by gravity-driven. This work presents a straightforward approach for preparing high-performance ion-exchange chromatography membranes for IgG separation.

Acid precipitation-hydrothermal synthesis of needle-like hydroxyapatite for protein adsorption from waste phosphogypsum

ABSTRACT In order to promote the high-value utilization of waste phosphogypsum (PG), hydroxyapatite was directly synthesized from PG by acid precipitation-hydrothermal method (PGHAP), which was used for the adsorption of bovine serum albumin (BSA) and lysozyme (LYS). The synthesized PGHAP was characterized by XRD, SEM, FTIR and BET, and the effects of various factors on protein adsorption capacity were studied. The results showed that PGHAP exhibits a clear needle-like morphology, high crystallinity, and an average size of about 200 nm. The pH had the greatest effect on the adsorption of protein, and the highest adsorption capacity was obtained at pH 4.0. In addition, the adsorption mechanism of protein on PGHAP was explored by adsorption kinetics and adsorption isotherm. The adsorption of protein on PGHAP conforms to the Intra-particle diffusion model kinetic model, the maximum adsorption capacity of protein on PGHAP can reach 31 mg/g, which is comparable to other adsorbents in this field. In addition, the adsorption behaviour of PGHAP on protein is more appropriately described by Langmuir isotherm model, which indicates that the binding site with uniform energy on the surface of PGHAP realizes the monolayer adsorption of protein. The main adsorption mechanisms are ion exchange, co-precipitation, complexation reaction and so on. Therefore, the needle-like PGHAP synthesized from waste PG is a protein adsorbent with industrial application potential.

Dialysis treatment, in vitro, and anticoagulation activity of polysulfone-polyacrylamide based-blend membranes: an experimental study.

The majority of treatments are performed with polysulfone (PSf) membranes. The main issue of the PSf membrane is its lack of endothelial function, leading to various processes like platelet adhesion, protein adsorption, and thrombus formation when comes in contact with blood. The crucial aspect in the development of hemodialysis (HD) membrane materials is a biocompatibility factor. This study aims to improve the performance and biocompatibility of PSf membranes by utilizing polyethylene glycol (PEG) as a pore-forming agent and polyacrylamide (PAA) as a multifunctional modifying additive owing to its non-toxic, and biocompatible nature. The formulated HD membranes were characterized using Fourier Transform Infrared (FTIR) spectroscopy, Scanning Electron Microscopy (SEM), and Water Contact Angle (WCA) measurements. The biocompatibility results showed that PSf-PAA membranes reduced the adsorption of bovine serum albumin (BSA) protein, hemolysis process, thrombus formation, and platelets adhesion with improved in vitro cytotoxicity results as well as anticoagulation performance. The protein separation results showed that PSf-PAA membranes were able to reject 90.1% and 92.8% of BSA protein. The membranes also showed better uremic waste clearance for urea (76.56% and 78.24%) and creatinine (73.71% and 79.13%) solutes, respectively. It is conceivable that these modern-age membranes may surpass conventional HD membranes regarding both efficiency and effectiveness.

Integration of highly sensitive large-area graphene-based biosensors in an automated sensing platform

Graphene-based biosensors, featuring exceptional electronic, mechanical, and surface properties, have emerged as frontrunners in advanced sensing technologies. However, to achieve widespread industrial adoption, advancements in the fabrication and integration of large-area graphene devices are essential. Critical parameters such as enhanced sensitivity, scalable production methods, economic viability, integration capabilities, and consistent uniformity must be meticulously addressed. In this work, we demonstrate that our ultra-clean, chemical wet transfer protocol of large-area graphene enables a scalable, smooth integration of graphene into an established assay platform for transporter protein drug discovery. Furthermore, we demonstrate sensitive detection of electrolytic buffers, varying pH, bovine serum albumin (BSA) and single-stranded DNA (ssDNA) adsorption, using our large-area graphene solution-gated field-effect transistor (SGFET) sensors, thereby proving their robust and reliable performance. The sensors’ biocompatibility and ion sensitivity, down to the picomolar range, substantiate their suitability for the investigation of electroactive transport in ion channels and membrane transporters.

Clicked into Place: Biomimetic Copolymer Adhesive for Covalent Conjugation of Functionalities.

Polydopamines (PDA) are a popular class of materials and promising candidates as adhesives for new fastening techniques. PDA layers can be formed on a wide range of substrates in various environments. Here, we present a novel method for functionalizing PDA-based copolymer films by using click chemistry. These copolymers adhere strongly to various surfaces and simultaneously have active groups that allow the attachment of functional groups. We discuss the coupling of two types of chitosan and a rhodamine B dye molecule to the alkyne groups of the copolymers by employing click reactions. Azidopropyl methacrylate (AzMA), methyl methacrylate (MMA), and dopamine methacrylamide (DOMA) are copolymerized and codeposited with (3-aminopropyl)triethoxysilane on silicon wafers, polyethylene (PE), and polytetrafluoroethylene (PTFE). AzMA provides the surfaces with azides for use in click reactions, MMA functions to control the polymer as a nonfunctional diluent, whereas DOMA provides adhesion, as well as cross-linking groups. After codeposition, the dyes are grafted to the copolymer to illustrate the ability of the films to link functional groups covalently. Fourier transform infrared spectroscopy confirms the successful click reaction in solution, and atomic force microscopy shows the surface morphologies following grafting. Fluorescence microscopy provides evidence of successful grafting. As an example of a possible application, layers exhibiting antifouling properties are prepared. Chitosan grafted to PE is tested for antifouling performance. These functionalized layers show nonspecific inhibition of protein adsorption. We find that chitosan can lower the adsorption of fluorescein-labeled bovine serum albumin (BSA) protein by more than 90% for the best performing fluorescein-labeled BSA protein and by more than 90% for the best-performing layer. These results demonstrate the viability of our PDA-based copolymers for surface functionalization through click chemistry grafting at challenging adhesion to surfaces.

In Vitro and In Vivo Evaluation of Toxicity of Structurally Different Diamond-Like Carbon Wear Debris in Joint Replacements.

Diamond-like carbon (DLC) wear debris, which is often composed of different types of structures, is generated from DLC-modified artificial joints in the human body, and its biocompatibility evaluation is especially important to prevent wear-debris-induced implant failure. Here, RAW 264.7 macrophages (inflammatory-reaction assay) and primary mouse osteoblasts (osteoblastogenesis assay) were employed to investigate the toxicity of DLC wear particles (DWPs) by evaluation of cell viability and morphology, enzyme-linked immunosorbent assays, and quantitative reverse-transcription polymerase chain reaction (PCR). Relevant histopathological analysis of rat joints was also performed in vivo. We found that DWPs with a relatively high sp2/sp3 ratio (graphite-phase tendency) manifested a higher cytotoxicity and significant inhibition of osteoblastogenesis. DWPs with a relatively low sp2/sp3 ratio (diamond-phase tendency) showed good biocompatibility in vivo. The DWPs exhibiting a low sp2/sp3 ratio demonstrated reduced secretion of TNF-α and IL-6, along with increased secretion of TIMP-1, resulting in the downregulation of MMP-2 and MMP-9 and upregulation of interleukin-10 (IL-10), thereby attenuating the inflammatory response. Moreover, coculturing osteoblasts with DWPs exhibiting a low sp2/sp3 ratio resulted in an elevated OPG/RANKL ratio and increased expression of OPG mRNA. Because of the absence of electrostatic repulsion, DWPs with a relatively low sp2/sp3 ratio enhanced bovine serum albumin adsorption, which favored cellular activities. Cytotoxicity assessment of DWPs can help establish an evaluation system for particle-related joint disease and can facilitate the clinical application of DLC-coated prostheses.

Deciphering BSA adsorption onto COL-BC: Interpretations from statistical physics modeling

In this current study, a single-energy double layer model was employed to inspect the adhesion mechanism of bovine serum albumin (BSA) on porous microsphere of cellulose (BC) collagen (COL) bacterium (COL-BC). Six physicochemical variables defining the retention mechanism, :the number of anchored BSA protein per site (n), the amount of (COL-BC) available pores (NM), the capacity of adsorbed quantity (Qa), the specific surface area (As), the concentrations at half saturation (C1/2) and the molar binding energy (ΔE1) are determined. Calculations revealed that n ≥ 1 indicating that an average of one BSA per site is linked to one (COL-BC) receptor site with forming two layers. The BSA/(COL-BC) docking system exhibits a weak binding affinity as evidenced by the computed molar adsorption energy (ΔE1) which is below 40 kJ/mol. This energetic observation aligns with the characteristics of a physical and exothermic binding mechanism. Analysis of the (COL-BC) surface using the Kelvin equation revealed a pore size distribution (PSDs) extending across 0.05 μm–2 μm, providing insights into the stereochemistry of its receptor sites. Discussion of the BSA/COL-BC adhesion reaction through Polanyi equation unveils an adsorption energy distribution (AED) localized between 0 and 15 kJ/mol, consistent with a weak interaction profile characteristic of a physisorption mechanism. Finally, three thermodynamic functions were estimated in order to macroscopically study the BSA/(COL-BC) adsorption systems.This work is involved to provide more information about the adsorption of BSA on the COL-BC microsphere and investigate a theorical approach for the application of the controlled release technology.

Synergistic effects of BSA adsorption and shear stress on corrosion behaviors of WE43 alloy under simulated physiological flow field

Protein adsorption first occurs for the blood-contacting bio-metallic stents, which plays essential roles in the biofilm formation and subsequent flow-induced corrosion. The synergistic effects of bovine serum albumin (BSA) and wall shear stress (WSS) on the corrosion of WE43 magnesium (Mg) alloy have been studied. The results indicate that BSA and WSS play competitive roles in accelerating the corrosion, specifically dominate under low WSS and a higher WSS respectively. Machine learning (ML) method is utilized to model the intrinsic corrosion mechanism. We expect this study might offer novel perspectives for better evaluating in vitro corrosion of Mg-based stents.

Stability Enhancement by Hydrophobic Anchoring and a Cross-Linked Structure of a Phospholipid Copolymer Film for Medical Devices.

Surface modification using zwitterionic 2-methacryloyloxyethylphosphorylcholine (MPC) polymers is one of the most reasonable ways to prepare medical devices that can suppress undesired biological reactions such as blood coagulation. Usable MPC polymers are hydrophilic and water soluble, and their surface modification strategy involves exploiting the copolymer structures by adding physical or chemical bonding moieties. In this study, we developed copolymers composed of MPC, hydrophobic anchoring moiety, and chemical cross-linking unit to clarify the role of hydrophobic interactions in achieving biocompatible and long-term stable coatings. The four kinds of MPC copolymers with cross-linking units, such as 3-methacryloxypropyl trimethoxysilane (MPTMSi), and four different hydrophobic anchoring moieties, such as 3-(methacryloyloxy)propyltris(trimethylsiloxy)silane (MPTSSi) named as PMMMSi, n-butyl methacrylate (BMA) as PMBSi, 2-ethylhexyl methacrylate (EHMA) as PMESi, and lauryl methacrylate as PMLSi, were synthesized and coated on polydimethylsiloxane, polypropylene (PP), and polymethyl pentene. These copolymers were uniformly coated on the substrate materials PP and poly(methyl pentene) (PMP), to achieve hydrophilic and electrically neutral coatings. The results of the antibiofouling test showed that PMBSi repelled the adsorption of fluorescence-labeled bovine serum albumin the most, whereas PMLSi repelled it the least. Notably, all four copolymers suppressed platelet adhesion similarly. The variations in protein adsorption quantities among the four copolymer coatings were attributed to their distinct swelling behaviors in aqueous environments. Further investigations, including 3D scanning force microscopy and neutron reflectivity measurements, revealed that the PMLSi coating exhibited a higher water intake under aqueous conditions in comparison to the other coatings. Consequently, all copolymer coatings effectively prevented the invasion of platelets but the proteins penetrated the PMLSi network. Subsequently, the dynamic stability required to induce shear stress was evaluated using a circulation system. The results demonstrated that the PMMMSi and PMLSi coatings on PMP and PP exhibited exceptional platelet repellency and maintained high stability during circulation. This study highlights the potential of hydrophobic moieties to improve hemocompatibility and stability, offering potential applications in medical devices.

Enhancement of antifouling and mechanical properties of polysulfone membrane using zwitterionic biphenyl polyimide as additive

Biphenyl polyimides, which are known by its excellent heat resistance and mechanical properties, were synthesized by adjusting the molar ratio of monomers, followed by end-functionalized with zwitterionic group via reaction with 1,3-propanesultone. The zwitterionic sulfobetaine biphenyl polyimide (z-biph-PI) copolymers with different hydrophobic chain lengths were employed as the additive for the preparation of polysulfone (PSf) membrane. X-ray photoelectron spectrometry (XPS) measurement on membrane surfaces revealed that the sulfobetaine groups of z-biph-PI migrated toward water in the membrane formation process, during which a large amount of porous, narrow and densely packed pores were created as illustrated in scanning electron microscopy (SEM) images. Therefore, the incorporation of z-biph-PI simultaneously enhanced the pure water flux and protein rejection ratio of membranes, overcoming the trade-off effects between permeability and selectivity. The adsorption of bovine serum albumin decreased from ∼47.7 μg/cm2 for the pristine membrane to a minimum of ∼12.4 μg/cm2 for the blend membrane. More importantly, the tensile strength and elongation at break were also simultaneously improved due to the unique mechanical property of biph-PI and the strong π-π interaction between biphe-PI and PSf. Meanwhile, the blend membrane exhibited excellent filtration and thermal stability. All these characteristics of the blend membrane made it promising in ultrafiltration application.

Reduction of polyketone membranes prepared by thermally induced phase separation with solvent co-extrusion for enhanced fouling resistance

This study utilized solvent co-extrusion technology and NaBH4 reduction to fabricate polyketone (PK) hollow fiber membranes with high water permeance and fouling resistance. Variations in reduction reaction time were explored to assess their impact on chemical composition, morphology, and properties. The results showed that the reduction reaction leads to the conversion of carbonyl groups on the membrane surface to hydroxyl groups, and with prolonged reaction time, the amount of hydroxyl groups on the membrane surface increases to a certain extent. The change in membrane chemical composition enhanced the hydrophilicity, while leaving the membrane morphology, mechanical properties, and separation performance largely unaffected. Static adsorption tests with bovine serum albumin (BSA) and E. coli exhibited distinct fouling behavior. While pristine PK membranes displayed significant BSA adsorption, PK reduction significantly reduced it. Both pristine and reduced PK membranes showed minimal E. coli attachment, likely due to weak interactions. Dynamic filtration tests demonstrated excellent flux recovery for reduced PK membranes, especially after 10 min of reduction, indicating superior fouling resistance with high flux recovery and low irreversible fouling, regardless of foulant type. These findings highlight a straightforward and efficient approach for producing high-performance membranes with exceptional fouling resistance suitable for practical applications.

Kinetic Relationships of the Adsorption of Lysozyme and Bovine Serum Albumin onto Zeolites of BEA and MFI Structural Types

Kinetic Relationships of the Adsorption of Lysozyme and Bovine Serum Albumin onto Zeolites of BEA and MFI Structural Types

Impact of Lipid Composition on Vesicle Protein Adsorption: A BSA Case Study.

Investigating the interaction between liposomes and proteins is of paramount importance in the development of liposomal formulations with real potential for bench-to-bedside transfer. Upon entering the body, proteins are immediately adsorbed on the liposomal surface, changing the nanovehicles' biological identity, which has a significant impact on their biodistribution and pharmacokinetics and ultimately on their therapeutic effect. Albumin is the most abundant plasma protein and thus usually adsorbs immediately on the liposomal surface. We herein report a comprehensive investigation on the adsorption of model protein bovine serum albumin (BSA) onto liposomal vesicles containing the zwitterionic lipid 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), in combination with either cholesterol (CHOL) or the cationic lipid 1,2-dioleoyl-3-trimethylammoniumpropane (DOTAP). While many studies regarding protein adsorption on the surface of liposomes with different compositions have been performed, to the best of our knowledge, the differential responses of CHOL and DOTAP upon albumin adsorption on vesicles have not yet been investigated. UV-vis spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed a strong influence of the phospholipid membrane composition on protein adsorption. Hence, it was found that DOTAP-containing vesicles adsorb proteins more robustly but also aggregate in the presence of BSA, as confirmed by DLS and TEM. Separation of liposome-protein complexes from unadsorbed proteins performed by means of centrifugation and size exclusion chromatography (SEC) was also investigated. Our results show that neither method can be regarded as a golden experimental setup to study the protein corona of liposomes. Yet, SEC proved to be more successful in the separation of unbound proteins, although the amount of lipid loss upon liposome elution was higher than expected. In addition, coarse-grained molecular dynamics simulations were employed to ascertain key membrane parameters, such as the membrane thickness and area per lipid. Overall, this study highlights the importance of surface charge and membrane fluidity in influencing the extent of protein adsorption. We hope that our investigation will be a valuable contribution to better understanding protein-vesicle interactions for improved nanocarrier design.

Titania Nanoparticles Doped Electrospun Membranes

Electrospun membranes exhibit very promising properties, such as high surface area, high surface area-to-pore volume ratio, high pore interconnectivity, and uniform pore distribution. Nanoparticles are a promising alternative for improving the properties of the electrospun membranes. Titania nanoparticles, which are stable, resistant, and non-toxic, have various applications including water treatment, sensors, food additive and cosmetics. Due to the high hydrophilicity of titania nanoparticles, membrane fouling is reduced in titania nanoparticles doped membranes. Titania nanoparticle doped polyacrylonitrile (PAN) nanocomposite electrospun membranes were prepared by electrospinning method in this work. Compared to bare PAN electrospun membranes 0.05% titania nanoparticles doped electrospun membranes have thinner nanofibers, higher hydrophilicity and almost 2 times lower bovine serum albumin adsorption, which shows lower fouling tendency.

Fluorescence study of the interaction between albumin and layered double hydroxides

Layered double hydroxides nanoparticles (LDH-NP) are increasingly studied for biomedical applications. Nevertheless, their interaction with biomolecules such as proteins needs further exploration for an effective application. In this work, the adsorption of bovine serum albumin (BSA) on LDH-NP and the conformation changes of the protein upon adsorption were characterized using fluorescence spectroscopy. First, the quenching of tryptophan residues of BSA by chloride-intercalated LDH-NP was explored and the BSA adsorption capacity of LDH-NP were determined. Then, the structural conformation of the protein was analyzed by fluorescence spectroscopy (including synchronous, polarization and quenching studies) at different surface coverages. Finally, the proclivity of adsorbed BSA molecules to assemble as amyloid fibril was evaluated. Due to the positive charging and low curvature of LDH-NP, BSA molecules were strongly adsorbed, which produced a quenching of the protein fluorescence and a large adsorption capacity. The effect on BSA conformation was dependent on surface coverage (SC): at low values ,t he tryptophan residues were in more hydrophobic environments and more accessible to quenchers than al high ones. At low SC, there is space between the BSA molecules to spread on the surface, which led to a conformation change. Contrarily, the native conformation around tryptophan residues of BSA was preserved at high SC due to the tight packing of the adsorbed protein molecules. As a result, BSA molecules are stabilized against the formation of amyloid fibrils at high SC, while at low SC they present a similar fibrillation than free BSA.

BSA Adsorption on Titanium Dioxide Nanoparticle Surfaces for Controlling Their Cellular Uptake in Skin Cells.

Nanoparticles (NPs) are continuously being developed for many applications including imaging, biomedicine, and everyday products. It is difficult to avoid contact with NPs such as titanium dioxide (TiO2) NPs, which are widely used in sunscreens. However, the safety of TiO2 NPs for skin contact and inhalation remains controversial. If NPs cannot penetrate the skin, they will be unable to circulate in the bloodstream, accumulate in the body, or cause side effects, ensuring their safety. Therefore, this study aimed to modify TiO2 NP surfaces to inhibit their uptake in skin cells. Inspired by protein corona studies, bovine serum albumin (BSA) was chosen to functionalize TiO2 NP surfaces via physical adsorption. The maximum BSA adsorption occurred at pH 5.0. The physicochemical properties (size, ζ-potential, morphology, ultraviolet (UV) absorption efficiency, and sun protection factor (SPF)) of TiO2-BSA NPs were comparable to those of TiO2 NPs, indicating that these properties did not affect cellular uptake. In the safety evaluation, TiO2 NPs and TiO2-BSA NPs exhibited high biocompatibility with skin cells and no phototoxicity after UVA and UVB irradiation. In the efficacy evaluation, both NPs possessed the same photoprotection abilities, reducing membrane damage and DNA breakage after UVA irradiation. Compared with TiO2 NPs, TiO2-BSA NPs showed substantially reduced skin penetration in Franz diffusion cells (91%) and human immortalized keratinocyte (HaCaT) cells (89%). A qualitative cellular uptake study using transmission electron microscopy and confocal laser scanning microscopy confirmed that TiO2 NPs were more abundant than TiO2-BSA NPs inside the HaCaT cells. These findings indicate that TiO2 surface functionalization with BSA inhibits cellular uptake in skin cells while maintaining safety and UV protection efficacy, which might be extended to other NP-based sunscreens.