Adsorption of Bovine Serum Albumin onto TiO2Particles

Giacomelli, Carla E.; Avena, Marcelo Javier; Pauli, Carlos P. De

doi:10.1006/jcis.1996.4750

Cited by 115 publications

(118 citation statements)

References 47 publications

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“…As it has been already pointed out, 18 the volume of washing solution is about 100 times that of the channel, which ensures a very efficient washing step. Adsorbed proteins don't desorb or desorb very slowly (hours): 34 consequently we assume that they are not removed during the washing step (the rate of desorption found in this study is -87 C eq /C max 6.7 6 10 22 -9 6 10 21 5.6 6 10 22 -0.89 Table 2 Comparison between the theoretical and the experimental C eq /C max reached in the microchannel of Fig. 1a.…”

Section: Reagents and Proceduresmentioning

confidence: 79%

Protein adsorption in static microsystems: effect of the surface to volume ratio

2005

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A numerical model for the adsorption kinetics of proteins on the walls of a microchannel has been developed using the finite element method (FEM) to address the coupling with diffusion phenomena in the restricted microchannel volume. Time evolutions of the concentration of one species are given, both in solution and on the microchannel walls. The model illustrates the adsorption limitation sometimes observed when the microdimensions of these systems induce a global depletion of the bulk solution. A new non-dimensional parameter is introduced to predict the final value of the coverage of any microsystem under static adsorption. A working curve and a criteria (h/KC max . 10) are provided in order to choose, for given adsorption characteristics, the value of the volume-to-surface ratio (i.e. the channel height h) avoiding depletion effects on the coverage (relative coverage greater than 90% of the theoretical one). Simulations were compared with confocal microscopy measurements of IgG antibody adsorption on the walls of a PET microchannel. The fit of the model to the experimental data show that the adsorption is under apparent kinetic control.

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Section: Reagents and Proceduresmentioning

confidence: 79%

Protein adsorption in static microsystems: effect of the surface to volume ratio

2005

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“…The adsorption of proteins onto TiO 2 NPs has been a subject of several studies. [18][19][20][21][22][23][24] In these studies, the connection between protein adsorption and cellular uptake was not investigated. Previously, we have evaluated the effect of physicochemical characteristics of a panel of TiO 2 NPs on uptake by fibroblasts.…”

Section: Introductionmentioning

confidence: 99%

The effect of blood protein adsorption on cellular uptake of anatase TiO2 nanoparticles

Allouni¹,

Gjerdet²,

Cimpan³

et al. 2015

IJN

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Protein adsorption onto nanoparticles (NPs) in biological fluids has emerged as an important factor when testing biological responses to NPs, as this may influence both uptake and subsequent toxicity. The aim of the present study was to quantify the adsorption of proteins onto TiO 2 NPs and to test the influence on cellular uptake. The surface composition of the particles was characterized by thermal analysis and by X-ray photoelectron spectroscopy. The adsorption of three blood proteins, ie, human serum albumin (HSA), γ-globulins (Glbs), and fibrinogen (Fib), onto three types of anatase NPs of different sizes was quantified for each protein. The concentration of the adsorbed protein was measured by ultraviolet-visible spectrophotometry using the Bradford method. The degree of cellular uptake was quantified by inductivity coupled plasma mass spectroscopy, and visualized by an ultra-high resolution imaging system. The proteins were adsorbed onto all of the anatase NPs. The quantity adsorbed increased with time and was higher for the smaller particles. Fib and Glbs showed the highest affinity to TiO 2 NPs, while the lowest was seen for HSA. The adsorption of proteins affected the surface charge and the hydrodynamic diameter of the NPs in cell culture medium. The degree of particle uptake was highest in protein-free medium and in the presence HSA, followed by culture medium supplemented with Glbs, and lowest in the presence of Fib. The results indicate that the uptake of anatase NPs by fibroblasts is influenced by the identity of the adsorbed protein.

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“…In a previous study, the amount of bovine serum albumin (BSA) adsorbed on colloidal TiO 2 particles was monitored as a function of pH, electrolyte concentration, and BSA concentration (29). The adsorption behavior could be explained by assuming that the BSA molecules adsorb without major conformational changes, forming a monolayer of adsorbed molecules that maintained the original size and shape that they had in solution.…”

Section: Introductionmentioning

confidence: 99%