Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity.

ABSTRACT: Physiochemical properties of engineered nanoparticles (NPs) play a vital role in nano-bio interactions, which are critical for nanotoxicity and nanomedicine research. To understand the effects of NP hydrophobicity on the formation of the protein corona, we synthesized four gold NPs with a continuous change in hydrophobicity ranging from -2.6 to 2.4. Hydrophobic NPs adsorbed 2.1-fold proteins compared to hydrophilic ones. Proteins with small molecular weights (<50 kDa) and negatively charge (PI < 7) constituted the majority of the protein corona, especially for hydrophobic NPs. Moreover, proteins preferred binding to hydrophilic NPs (vitronectin and antithrombin III), hydrophobic NPs (serum albumin and hemoglobin fetal subunit beta), and medium hydrophobic NPs (talin 1 and prothrombin) were

SUBMITTER: Yu Q 

PROVIDER: S-EPMC7100549 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature