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In Nanotechnology: Protein Corona Formation on Magnetic Nanoparticles (together with Silvio Dutz and Joachim Clement)

The inevitable formation of a protein corona upon contact of nanoparticles with different biological fluids is of great interest in the context of biomedical applications. It is well established that the surface chemistry of the respective nanomaterial has tremendous impact on protein adsorption, both in terms of the actual amount as well as the type of proteins adsorbed. In that regard, especially polyzwitterions are discussed as coating materials as they are known to partially inhibit protein adsorption. We herein present comparative incubation studies on iron oxide nanoparticles (either single core (SPION) or multicore nanoparticles (MCNP)) after coating with either polyanionic or polyzwitterionic polymeric shells based on polydehydroalanine (PDha). Apart from varying surface charge and chemistry, also the influence of incubation time and temperature on the formation and composition of a protein corona upon exposure to fetal calf serum (FCS) was investigated. The amounts of adsorbed biomolecules were determined using thermogravimetric analysis (TGA). SDS-PAGE experiments revealed information on protein composition as major components of the biomolecule corona. Our results show that distinctly lower amounts of proteins are adsorbed onto polyzwitterionic hybrid nanoparticles in general, but also the corona composition varies as indicated by elevated relative ratios of medium molecular weight proteins (i.e. proteins 25-100 kDa) estimated by non-specific silver protein staining. In addition, increasing relative amounts of albumin (67 kDa) via specific Western blot assays on PDha-coated MCNP are detected.

Original Article:

C. Gräfe, M. von der Lühe, A. Weidner, P. Globig, J. H. Clement, S. Dutz, F. H. Schacher, "Protein Corona Formation and its Constitutional Changes on Magnetic Nanoparticles in Serum Featuring a Polydehydroalanine Coating: Effects of Charge and Incubation Conditions", Nanotechnology 2019, in press

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