Electrokinetic Hummel-Dreyer characterization of nanoparticle-plasma protein corona: The non-specific interactions between PEG-modified persistent luminescence nanoparticles and albumin.

Colloids Surf B Biointerfaces

PSL Research University, Chimie ParisTech, Unité de Technologies Chimiques et Biologiques pour la Santé, 75005, Paris, France; INSERM, Unité de Technologies Chimiques et Biologiques pour la Santé (U 1022), 75006, Paris, France; CNRS, Unité de Technologies Chimiques et Biologiques pour la Santé UMR 8258, 75006, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, Unité de Technologies Chimiques et Biologiques pour la Santé, 75006, Paris, France. Electronic address:

Published: November 2017

Nanoparticles (NPs) play an increasingly important role in the development of new biosensors, contrast agents for biomedical imaging and targeted therapy vectors thanks to their unique properties as well as their good detection sensitivity. However, a current challenge in developing such NPs is to ensure their biocompatibility, biodistribution, bioreactivity and in vivo stability. In the biomedical field, the adsorption of plasmatic proteins on the surface of NPs impacts on their circulation time in blood, degradation, biodistribution, accessibility, the efficiency of possible targeting agents on their surface, and their cellular uptake. NP surface passivation is therefore a very crucial challenge in biomedicine. We developed herein for the first time an electrokinetic Hummel-Dreyer method to quantitatively characterize the formation of protein corona on the surface of NPs. This strategy was designed and optimized to evaluate the non specific binding of bovine serum albumin with the recently discovered PEG-functionalized ZnGaCrO persistent luminescence NPs developed for in vivo biological imaging. The binding strength and the number of binding sites were determined at different ionic strengths. This methodology opens the way to an easy, low sample- and low time-consuming evaluation of the impact of NP surface modification on protein-corona formation and therefore on their potential for various bio-medical applications.

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http://dx.doi.org/10.1016/j.colsurfb.2017.08.012DOI Listing

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