Abstract
Understanding the interactions of serum proteins to surfaces are of paramount importance to the domain of nano-drug delivery systems. At the nano-bio interface, human plasma differentially interacts with engineered nanomaterials through the creation of protein coronas, which in turn become primary determinants of both the pharmacokinetics and pharmacodynamics of the circulating nanoparticles. Here, for the first time, the specific binding kinetics of the four major corona forming proteins (human serum albumin, fibrinogen, ApoA1, and polyclonal IgG) are determined for gold nanoparticles (AuNPs). Using a multiplexed surface plasmonic assay, highly reproducible measurements of on rate (kon), off rate (koff), and dissociation constant (KD), in addition to relative amounts of protein binding, were obtained. Dramatic differences in kon for individual components were shown as primary determinants of protein affinities, with kon ranging over nearly two orders of magnitude for the proteins studied, while koff remained within a factor of two for the set. The effect of polyethylene glycol (PEG) modification on plasma component binding was also studied and the effect of PEG length on human serum interaction was characterized through systematic screening of PEG molecular weight (2–30 K). The effect of nanoparticle modification on particle targeting was also characterized through study of a hybrid AuNP system.
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Patra, A. (2017). Quantifying Interactions Between Serum Proteins and Gold Nanoparticles. In: Quantifying Interactions of Biomolecules with Inorganic Surfaces. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-30728-2_5
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DOI: https://doi.org/10.1007/978-3-319-30728-2_5
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