ABSTRACT

This chapter reanalyzes data from a panel of nine published studies. It suggests that hydrophobicity of proteins is an important parameter for their adhesive properties, subsets of proteins identified in corona should be considered as interactomes, namely, proteins linked by explainable biological interplays that were recently called coronome, a contraction of corona proteome, and InterPro Domains (IPD) of proteins reflect protein–protein or protein–NP interactions well and should be extensively determined by protein identification using MS tools. There is a considerable interest in changes of the physicochemical properties of nanoparticles (NP) once they are surrounded by biological media. To target cells efficiently and to avoid being cleared by scavenger cells like macrophages, many researchers in nanomedicine are looking for their "stealth" property in biological fluids. The notion of "biological identity" or protein fingerprinting of NP, driven by the discovery of adhesion forces between specific proteins of biological fluids and NP, emerged in studies published recently.