Abstract
Colloidal nanoparticles (NPs) are a versatile potential platform for in vivo nanomedicine. Inside blood circulation, NPs may undergo drastic changes, such as by formation of a protein corona. The in vivo corona cannot be completely emulated by the corona formed in blood. Thus, in situ detection in complex media, and ultimately in vivo, is required. Here we present a methodology for determining protein corona formation in complex media. NPs are labeled with 19F and their diffusion coefficient measured using 19F diffusion-ordered nuclear magnetic resonance (NMR) spectroscopy. 19F diffusion NMR measurements of hydrodynamic radii allow for in situ characterization of NPs in complex environments by quantification of protein adsorption to the surface of NPs, as determined by increase in hydrodynamic radius. The methodology is not optics based, and thus can be used in turbid environments, as in the presence of cells.
Highlights
Colloidal nanoparticles (NPs) are a versatile potential platform for in vivo nanomedicine
Several optical methods, such as fluorescence correlation spectroscopy (FCS)[6] or depolarized dynamic light scattering (DDLS)[7], have been established for in situ quantification based on diffusion coefficient measurements
In complex media such as rh(NHSA/NP) blood or even tissue, optical detection suffers from light scattering
Summary
Colloidal nanoparticles (NPs) are a versatile potential platform for in vivo nanomedicine. The dynamic development of protein corona formation has been studied extensively by mass spectroscopy or other techniques[3] Such measurements have been performed in relevant solutions such as blood[4], which, requires extraction of the NPs and removal of unbound excess proteins, leading to a loss of the equilibrium properties[5]. In case only b protein–NP complexes, but no free proteins, are subject to diffusion coefficient measurements, protein corona formation can be quantified in situ, without removal of excess proteins[6,7] Several optical methods, such as fluorescence correlation spectroscopy (FCS)[6] or depolarized dynamic light scattering (DDLS)[7], have been established for in situ quantification based on diffusion coefficient measurements. NMR has long been used for structural studies of proteins[10,11]; we propose the c use of 19F diffusion NMR to observe changes in hydrodynamic radius of NPs upon adsorption of proteins in solution and in complex media such as blood
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