Physical insight into novel lipid corona formation and its impact on the interaction with protein

Abstract

The coating of proteins and lipids around nanoparticle surfaces is known as the “protein corona” and “lipid corona” respectively. While protein corona formation is well-studied [1,2], the mechanism and stability of lipid corona formation are less understood and have recently attracted attention in nanoscience. Although some studies emphasize the role of electrostatic forces between nanoparticles (NPs) and lipid vesicles in lipid corona formation [3,4], little is known about the specific roles of physicochemical properties of NPs and lipids that influence this process. This thesis uses aromatic amino acid-functionalized NPs as model systems to interact with lipid vesicles based on following the hypothesis. In some virus particles, the capsid, made of protein, encases the viral genome (either DNA or RNA) with lipid membrane wrapping. Given that amino acids are the building blocks of proteins, it is plausible to hypothesize that amino acids could self-assemble on the surface of NPs and potentially attract lipid molecules from membranes to form a lipid coating, or "lipid corona”. The thesis provides a detailed exploration of lipid corona formation, focusing on the influence of lipid (charge, concentration, phase state, chain length, hydrophobicity, and head group area) and NPs properties (surface charge, surface ligands functionalization, and metallic core).