A quantitative binding study of fibrinogen and human serum albumin to metal oxide nanoparticles by surface plasmon resonance

Abstract

The interaction of plasma proteins with metal oxide nanoparticles (NPs) is important due to the potential biomedical application of these NPs. In this study, new approaches were applied to measure quantitatively the kinetics and affinities of fibrinogen and human serum albumin (HSA) for TiO2, CeO2, Al2O3 and ZnO NPs immobilized on a sensor chip. Real-time surface plasmon resonance (SPR) measurements showed that fibrinogen interacted with TiO2 and CeO2 NPs with high affinity (135 and 40 pM, respectively) and to Al2O3 NPs with moderate affinity (15 nM). The data fitted well to the Langmuir model describing a 1:1 interaction. In contrast, HSA interacted with TiO2, CeO2 and Al2O3 NPs with lower affinity (80 nM, 37 nM and 2 µM, respectively) with the data fitting better to the conformational change model. TiO2 and CeO2 NPs had fast association rate constants with fibrinogen (1×10(6) M(-1) s(-1)) and Al2O3 NPs had a slower association rate constant (1×10(4) M(-1) s(-1)). By contrast, HSA had markedly slower association rate constants (1×10(3)-1×10(4) M(-1) s(-1)). The binding of the proteins was reversible, thus allowing the rapid capture of data for replicates. The occurrence of matrix effects was evaluated by using surfaces with different chemistries to capture the NPs, namely alginate, NeutrAvidin and bare gold. The affinity values determined for the NP-protein interactions were largely independent of the underlying surface used to capture the NPs.

Dissociation coefficients of protein adsorption to nanoparticles as quantitative metrics for description of the protein corona: A comparison of experimental techniques and methodological relevance

“…However, since this methodology implies the chemical coupling of NPs or proteins to the solid support (cheap) of the SPR device a major problem might be the interference of the chemical nature of this supporting matrix with protein-NP interaction. Canoa et al [51] applied SPR to obtain the affinity Isothermal titration calorimetry (ITC) ITC is a very informative label-free method that allows for obtaining both affinity and maximal binding capacity of a certain ligand to NPs, by the detection of the generated, or adsorbed, heat. The measured thermal exchanges may be due to the formation of protein-NPs complexes but also to possible protein denaturation events that also contribute in determining K D values.…”

“…With all the caveats emerged, the available data indicate that zeta-potential of the NPs thus seems to be a very influential parameter. [24,35,50,51]. The yellow line acts merely as a guide to the eye to follow the trend of data, without analytical rational behind the shape of the curve.…”

Investigation of biological cell–small molecule interactions with a gold surface plasmon resonance sensor using a laser scanning confocal imaging-surface plasmon resonance system

“…[28][29][30][31] Commercial instruments based on SPR theory have been developed and extensively used to trace contaminants in water, food, and air because of the highly sensitive optical reflectivity of gold film to dielectric changes in environment. 38,39 Detecting small molecule-biologic cell interaction directly and effectively is still a challenge. 36,37 However, small molecule-biologic cell interaction is difficult to investigate using free-labeled method because of their low molecular weight, although interactions of a few small molecules have been achieved through special modification with large molecules or nanoparticles.…”

The influence of the sequence of nanoparticles injection to solution on the rate of fibrinogen-thrombin reaction

“…In Figure 1 also presents values of amplitudes of correlation function of intensity g (2) (τ) and the total intensities of scattered light (I/IL). In gel formation before sol-gel transition the total intensity of scattered light (I/IL) increases sharply, while the amplitude of correlation function decreases and the correlation function has such a shape, which gives a set of consecutive times or sizes being decomposed by exponents (Figures 1e,f).…”

“…They can be used for target and drug delivery, for visualization of metastasis, for stimulation of angio-and arteriogenesis, etc. Many papers are devoted to the investigations of nanoparticle interactions with proteins, for example, study of binding mechanism of Fe 2 O 3 nanoparticles with fibrinogen by using a combination of circular dichroism, UVvis fluorescence spectroscopic and computational methods [1]; or surface plasmon resonance study of fibrinogen and human serum albumin binding to metal oxide nanoparticles [2], etc. However, influencing of the nanoparticles on the rate of important biological reaction is not fully studied yet.…”