Nanoparticles (NPs) in contact with biological fluids are immediately coated by a protein corona (PC), composed of hard (strongly bounded) and/or soft (loosely associated) protein layers. The PC governs the biological ‘identity’ of a NP and represents the actual nano-interface that is presented to and interacts with cellular membranes. Understanding such interactions can be used to design nanomaterials with controlled surface characteristics in a biological environment. In this regard, lipid monolayers employed as model membranes have been extensively used to examine interactions between bio-membranes and NPs. In this work, we combined Langmuir Blodgett technique with hyperspectral microscopy to investigate how the NP-cell membrane interactions are modulated by the presence of a protein (human serum albumin), either free in the environment or included in the hard and soft coronas, and to explore their effects on the formation and structure of lipid domains. Our results show that the inclusion of 100 nm polystyrene (PS) nanoparticles within a monolayer does not affect the monolayer lipid packing and phase state. Complexation of the PS NPs with proteins promotes their attachment to the lipid monolayers. PS NPs-hard corona (HC) complexes cause lipid extraction at high monolayer surface pressure (30 mN m<sup>-1</sup>) and lead to the modification of the monolayer phase behavior with hindering of growth of solid domains, increasing of the monolayer resistance to compression, and lowering of the collapse pressure. We also found that NPs-soft corona (SC) complexes, thus far not considered important for such interactions, induced greater changes in lipid monolayer structure than the NPs alone at the same concentration. Compared to NP-HC complexes, NP-SC complexes yield more disordered structure in monolayers with less cohesion between the lipid molecules.  <br/>

Protein coronas enhance polystyrene interactions with a model human erythrocyte membrane outer leaflet

255th National Meeting (2018)

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