Protein corona formation on nanoparticles with different surface chemistry

Abstract

Nanomaterials have found extensive application in medicine, biology, and the chemical industry, which has led to a growing interest in exploring their behavior within biological environments. In recent years, significant progress has been made in the physical and chemical modification of biomaterial surfaces to enhance their interactions with complex biological environment. There is urgent need to focus on studying the interactions between nanomaterial surfaces and biological environments in order to provide essential insights for enhancing performance and advancing the applications of nanomaterials. This thesis presents a comprehensive investigation into the protein corona formation, which illustrates the dynamic interaction between nanoparticles and proteins. First, various surface chemical modifications were performed on quantum dots with intrinsic fluorescence properties to endow them with different surface physicochemical characteristics, such as surface charge and hydrophilicity. Subsequently, these modified quantum dot-based nanoparticles were exposed to specific proteins under varying pH conditions. Fluorescence correlation spectroscopy (FCS) was used to track the formation process of protein corona on the surface of the nanoparticles, providing us with systematic and accurate understanding of protein corona formation. Protein corona formation is a multifaceted process influenced by various factors, including the properties of the nanomaterial, the type of protein, and the specific biological environment. By investigating the dynamic process of protein corona formation under distinct conditions, we can gain a deeper and more comprehensive understanding of the determinants behind this phenomenon. This knowledge enables us to effectively modulate the formation of protein corona, either to mitigate or enhance it, in the design and utilization of nanomaterials in diverse application.