Protein corona modulates interaction of spiky nanoparticles with lipid bilayers

• Published in: Journal of colloid and interface science Vol. 603; pp. 550 - 558
• Main Authors: Fleury, Jean-Baptiste, Werner, Marco, Guével, Xavier Le, Baulin, Vladimir A.
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01.12.2021; Elsevier
• Subjects: Chemical Sciences; Engineering Sciences; Lipid bilayers; Microfluidics; Nanoparticles; Nanostars; Pore formation; Protein corona; Nanoparticles; Nanostars; Protein corona; Lipid bilayers; Microfluidics; Pore formation
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/j.jcis.2021.06.047

[Display omitted] The impact of protein corona on the interactions of nanoparticles (NPs) with cells remains an open question. This question is particularly relevant to NPs which sizes, ranging from tens to hundreds nanometers, are comparable to the sizes of most abundant proteins in plasma. Protein sizes match with typical thickness of various coatings and ligands layers, usually present at the surfaces of larger NPs. Such size match may affect the properties and the designed function of NPs. We offer a direct demonstration of how protein corona can dramatically change the interaction mode between NPs and lipid bilayers. To this end, we choose the most extreme case of NP surface modification: nanostructures in the form of rigid spikes of 10–20 nm length at the surface of gold nanoparticles. In the absence of proteins we observe the formation of reversible pores when spiky NPs adsorb on lipid bilayers. In contrast, the presence of bovine serum albumin (BSA) proteins adsorbed at the surface of spiked NPs, effectively reduces the length of spikes exposed to the interaction with lipid bilayers. Thus, protein corona changes qualitatively the dynamics of pore formation, which is completely suppressed at high protein concentrations. These results suggest that protein corona can not only be critical for interaction of NPs with membranes, it may change their mode of interaction, thus offsetting the role of surface chemistry and ligands.