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

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