Albumin adsorption influence on the stability of the mesoporous zirconia suspension

Szewczuk-Karpisz, Katarzyna; Wiśniewska, Małgorzata; Myśliwiec, Dawid

doi:10.1016/j.jiec.2015.08.005

Cited by 17 publications

(8 citation statements)

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“…The hydrophobicity map was produced using the hydrophaty index. 14 Recent experimental BSA adsorption studies [15][16][17][18][19][20] have revealed numerous interesting phenomena regarding this protein's behaviour at the surface. However, even modern experimental techniques in isolation have limited access to molecular details such as:…”

Section: Figure1mentioning

confidence: 99%

“…Recent experimental BSA adsorption studies − have revealed numerous interesting phenomena regarding this protein’s behavior at the surface. However, even modern experimental techniques in isolation have limited access to molecular details, such as Identifying the most important residues and their interactions with the surface, the water, and the ions close to the surface; Understanding how a negative protein, such as BSA at pH7, can adsorb to a negatively charged surface, such as silica at pH7; Determining the final protein orientation and conformation on the surface; Distinguishing the roles of the various forces and interactions; Assessing the adsorbed protein’s mobility and diffusion pathways on the surface; Compiling a complete molecular-scale picture of the structure and properties of adsorbed protein layers. …”

Section: Introductionmentioning

confidence: 99%

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Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

et al. 2017

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Molecular details of BSA adsorption on a silica surface are revealed by fully atomistic molecular dynamics (MD) simulations (with a 0.5 μs trajectory), supported by dynamic light scattering (DLS), zeta potential, multiparametric surface plasmon resonance (MP-SPR), and contact angle experiments. The experimental and theoretical methods complement one another and lead to a wider understanding of the mechanism of BSA adsorption across a range of pH 3-9. The MD results show how the negatively charged BSA at pH7 adsorbs to the negatively charged silica surface, and reveal a unique orientation with preserved secondary and tertiary structure. The experiments then show that the protein forms complete monolayers at ∼ pH6, just above the protein's isoelectric point (pH5.1). The surface contact angle is maximum when it is completely coated with protein, and the hydrophobicity of the surface is understood in terms of the simulated protein conformation. The adsorption behavior at higher pH > 6 is also consistently interpreted using the MD picture; both the contact angle and the adsorbed protein mass density decrease with increasing pH, in line with the increasing magnitude of negative charge on both the protein and the surface. At lower pH < 5 the protein starts to unfold, and the adsorbed mass dramatically decreases. The comprehensive picture that emerges for the formation of oriented protein films with preserved native conformation will help guide efforts to create functional films for new technologies.

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Section: Figure1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

et al. 2017

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“…8,19−21 pH can influence protein adsorption on nanoparticle surfaces. 22 It has been reported that protein adsorption is optimal at its isoelectric point 23,24 as the protein−protein interaction is minimized and electrostatic repulsion is reduced, which enables compact protein molecules to pack onto the surface to the greatest extent. 25,26 Phosphate in blood and in buffer solution provides a pHstable environment.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Below pH 3.5, BSA adopts a more extended form (E-form) and expands to an oblate spheroid shape . The dimensions of N-from, F-form, and E-from BSA are 8.0 × 8.0 × 3.0 Å, 4.0 × 4.0 × 12.9 Å, and 2.1 × 2.1 × 25.0 Å, respectively. , Furthermore, proteins can undergo conformational changes upon surface adsorption. ,− pH can influence protein adsorption on nanoparticle surfaces . It has been reported that protein adsorption is optimal at its isoelectric point , as the protein–protein interaction is minimized and electrostatic repulsion is reduced, which enables compact protein molecules to pack onto the surface to the greatest extent. , …”

Section: Introductionmentioning

confidence: 99%

Bovine Serum Albumin Adsorption on TiO₂ Nanoparticle Surfaces: Effects of pH and Coadsorption of Phosphate on Protein–Surface Interactions and Protein Structure

Grassian

2017

J. Phys. Chem. C

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Protein adsorption on nanoparticle surfaces plays a critical role in biological systems, and bovine serum albumin (BSA) is a useful model protein to study due to its high abundance and similar properties as its human variant. Herein, a quantitative understanding of the interaction between titanium dioxide (TiO 2 ) nanoparticle (22 nm average diameter) and BSA was carried out to explore the effect of pH on surface coverage and adsorbed protein structure. Experiments were conducted under different pH conditions (pH 7.4, 4.5, and 2.0) that simulate the pH of blood, lung, and stomach fluids, respectively. Attenuated total reflectance−Fourier transform infrared (ATR-FTIR) spectroscopy was used for in situ adsorption characterization and protein secondary structure analysis. In addition, thermogravimetric analysis (TGA) was used to provide quantitative determination of the surface coverage. These results show that BSA adsorption on TiO 2 highly depends on pH as well as the presence of salts. Furthermore, it is also shown that coadsorbed phosphate ion reduces the amount denaturation of BSA on TiO 2 at acidic pH. Thus, the results of this study provide new insights into understanding protein behavior on nanoparticle surfaces at different pH in the presence and absence of coadsorbed phosphate.

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“…Adsorption of BSA to various surfaces such as gold nanoparticles, gold electrodes, polypyrrole-based adsorbents, neutral and charged hydrophilic and hydrophobic surfaces, silica, poly(hydroxyethylmethacrylate)-Reactive Green 19 cryogel disks, mica, polymeric nanoparticles, chromium(III) oxide suspension, zirconia nanoparticles were investigated in some of the reported literature studies [14][15][16][17][18][19][20][21][22][23]. In recent years, there are only a few studies related with the investigation of the adsorption and the attractions between the proteins and carbon based nanomaterials [5,[21][22][23][24][25][26][27][28][29].…”

Section: Introductionmentioning

confidence: 99%

Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system

Kopaç

Bozgeyik

Flahaut

2018

Journal of Molecular Liquids

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Adsorption and interactions of Bovine Serum Albumin (BSA) with Double Walled Carbon Nanotubes (DWNT) prepared by catalytic chemical vapor deposition (CCVD) synthesis were studied. Adsorption kinetics and equilibrium were investigated by means of in situ UV-spectroscopy. The extent of adsorption at different temperatures was determined at the end of a 420-min adsorption period. The adsorption equilibrium experiments were performed using various amounts of nanotubes at pH 4 and 40°C, and the adsorption parameters were evaluated comparing the experimental data with models such as the Freundlich and Langmuir isotherms. The maximum protein adsorption capacity (Q 0) of DWNT was determined as 1221 mg•g −1. The effect of temperature on the adsorption rate experiments was investigated for constant amount of adsorbent at pH 4. Adsorption kinetics followed the pseudo-first-order rate. Zeta potential measurements were performed with respect to solution pH for understanding the protein-surface interactions. The interactions between positively charged BSA molecules with negatively charged DWNT at pH 4 were found to be electrostatic attractions. Thermodynamic parameters, ΔH 0 and ΔS 0 were found as 9.40 kJ•mol −1 and 321.5 J•mol −1 K −1 , respectively. ΔH 0 value indicated that BSA adsorption on DWNT was a physisorption process.

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Albumin adsorption influence on the stability of the mesoporous zirconia suspension

Cited by 17 publications

References 38 publications

Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

Bovine Serum Albumin Adsorption on TiO₂ Nanoparticle Surfaces: Effects of pH and Coadsorption of Phosphate on Protein–Surface Interactions and Protein Structure

Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system

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Albumin adsorption influence on the stability of the mesoporous zirconia suspension

Cited by 17 publications

References 38 publications

Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment

Bovine Serum Albumin Adsorption on TiO2 Nanoparticle Surfaces: Effects of pH and Coadsorption of Phosphate on Protein–Surface Interactions and Protein Structure

Adsorption and interactions of the bovine serum albumin-double walled carbon nanotube system

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Product

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Bovine Serum Albumin Adsorption on TiO₂ Nanoparticle Surfaces: Effects of pH and Coadsorption of Phosphate on Protein–Surface Interactions and Protein Structure