Abstract
Understanding the effects mediated by a set of nanoparticle (NP)-bound host biomolecules, often indicated with the umbrella term of NP corona, is essential in nanomedicine, nanopharmacology, and nanotoxicology. Among the NP-adsorbed proteome, some factors mediate cell binding, endocytosis, and clearing by macrophages and other phagocytes (opsonins), while some others display few affinities for the cell surface (dysopsonins). The functional mapping of opsonins and dysopsonins is instrumental to design long-circulating and nanotoxicologically safe next-generation nanotheranostics. In this review, we critically analyze functional data identifying specific proteins with opsonin or dysopsonin properties. Special attention is dedicated to the following: (1) the simplicity or complexity of the NP proteome and its modulation, (2) the role of specific host proteins in mediating the stealth properties of uncoated or polymer-coated NPs, and (3) the ability of the innate immune system, and, in particular, of the complement proteins, to mediate NP clearance by phagocytes. Emerging species-specific peculiarities, differentiating humans from preclinical animal models (the murine especially), are highlighted throughout this overview. The operative definition of opsonin and dysopsonin and the measurement schemes to assess their in vitro efficacy is critically re-examined. This provides a shared and unbiased approach useful for NP opsonin and dysopsonin systematic identification.
Highlights
In this review, we summarize the present-day knowledge concerning host proteins able to up- or downmodulate the capture of nanoparticles (NPs) by phagocytes and other cells
In section “Re-examination of the Complexity of the NP Proteome Composition,” we address major methodological and conceptual issues relevant to assess the composition of the whole set of proteins binding to NPs
In section “Opsonin-Dysopsonin Balance on Nanoparticles and Its Tilting by Complement,” we eventually present our view on the dynamic interplay between the different host-derived proteins interacting at the bio-nano interface
Summary
We critically analyze functional data identifying specific proteins with opsonin or dysopsonin properties. Special attention is dedicated to the following: [1] the simplicity or complexity of the NP proteome and its modulation, [2] the role of specific host proteins in mediating the stealth properties of uncoated or polymercoated NPs, and [3] the ability of the innate immune system, and, in particular, of the complement proteins, to mediate NP clearance by phagocytes. The operative definition of opsonin and dysopsonin and the measurement schemes to assess their in vitro efficacy is critically re-examined. This provides a shared and unbiased approach useful for NP opsonin and dysopsonin systematic identification.
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