PEGylated lipids impede the lateral diffusion of adsorbed proteins at the surface of (magneto)liposomes.

Protein binding to nanoparticles is a crucial issue in biomedicine, as it triggers their clearance from the bloodstream after intravenous injection. Many techniques are available for measuring strong protein binding interactions, but weak dynamic interactions are more difficult to assess. To tackle the latter problem, in the present work, cytochrome c was chosen as a representative model of a water-soluble protein and the adsorbing particulates were either small unilamellar phospholipid vesicles or 14nm diameter solid superparamagnetic iron oxide cores onto which a phospholipid bilayer was strongly chemisorbed (so-called magnetoliposomes). Incorporation of cytochrome c oxidase into the phospholipid bilayer allowed the association of cytochrome c with the surface of the particles to be measured with high sensitivity by VIS-spectrophotometry. The impact of enzyme density as well as some of the physical features of the PEG corona (degree of PEGylation and PEG chain length) adjacent to the surface of the lipid structures on the overall kinetics was also investigated.