Abstract
AbstractThe surface interactions of nanoparticles (NPs) with proteins are intensively studied because they partly determine the biological fate of these reagents. The protein interaction trajectory of NPs delivered from complex biofluids into the cytosol of vertebrate cells however remains poorly characterized. This topology is explored using isolated whole cytoplasm and carboxylated superparamagnetic iron oxide NPs (SPIONs). SPIONs are introduced into the cytoplasm in naked form or with an adsorbed cargo of serum proteins as an example of a complex NP “corona.” By filtering interactome datasets with information about protein localization and absolute cytosolic concentration, the soluble cytoplasmic proteins that contribute to corona formation in the cytoplasm are identified. These include a subset of glycolytic enzymes and proteins in soluble ribosomes. In the cytoplasm, the proteins of the serum corona are quickly removed from SPIONs by a non‐proteolytic mechanism. Although naked SPIONs and SPIONs with a serum corona capture the same 65 cytosolic proteins, their overall interaction trajectory in the cytoplasm is not identical. In particular, they diverge in engagement with macroscale cell parts such as mitochondria. This knowledge of the interaction landscape of NPs in the cytoplasm is expected to support hypothesis development in projects aimed at improving NP reagents for biomedical applications.
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