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Facile evaluation of nanoparticle-protein interaction based on charge neutralization with pulsed streaming potential measurement.

Exploration of simple and universal methods to quantitatively measure nanoparticle (NP)-protein interaction is of great importance. In this work, pulsed streaming potential (SP) measurement has been used to evaluate the interaction between NPs and proteins within microchannels. Graphene oxide (GO) and SiO2 NPs were selected to represent two kinds of NPs. Lysozyme and common blood proteins, including albumin V, γ-globulins, and fibrinogen were used as model proteins. The linear relationship between the initial adsorption rate (S = dEr/dt) and the concentration of proteins was observed. Combined with the Hill equation, the microscopic dissociation constant (KD) and the Hill coefficient (n) between NPs and proteins were calculated based on the relationship between S and the concentration of each protein. The concentration of free proteins which are not interacted with the NPs in the NPs-protein mixture could also be measured. The influence of pH, conductivity, and ionic strengths of the incubation buffer on the interaction between GO and lysozyme was evaluated based on the constant KD. The interaction intensity between NPs and proteins was defined as charge neutralization efficiency QC, which could be calculated from the value of S. It takes only 150 s to get the whole set of data under the optimized experiment parameters. The measurement solely depends on the surface charge, no intrinsic fluorescence is required for either the NPs or the proteins, and no labeling or immobilization process is involved as well.