Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7231782 | Biosensors and Bioelectronics | 2015 | 8 Pages |
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 (1Ã106 Mâ1 sâ1) and Al2O3 NPs had a slower association rate constant (1Ã104 Mâ1 sâ1). By contrast, HSA had markedly slower association rate constants (1Ã103-1Ã104 Mâ1 sâ1). 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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Pilar Canoa, Rosana Simón-Vázquez, Jonathan Popplewell, África González-Fernández,