Protein Corona Formed from Different Blood Plasma Proteins Affects the Colloidal Stability of Nanoparticles Differently.
Authors of this article are:
Ho YT, Azman N’, Loh FWY, Ong GKT, Engudar G, Kriz SA, Kah JCY.
A summary of the article is shown below:
Significant progress in the characterization of the protein corona has been made. However, insights on how the corona affects the aggregation of nanoparticles (NPs) and hence its biological identity are still lacking. Here, we focused on elucidating how the corona formed from four major serum proteins: immunoglobulin G (IgG), fibrinogen (FBG), apolipoprotein A1 (ApoA1), and human serum albumin (HSA) over a range of concentrations affect the aggregation of gold NPs (AuNPs). We found that at physiological pH of 7.4, all four proteins aggregated the AuNPs at low concentrations but conferred colloidal stability at high concentrations due to the complete “corona coat” around individual AuNP. Due to their immune-related functions, IgG and FBG aggregated the AuNPs to a greater extent compared to HSA and ApoA1 which were mostly involved in transport of small molecules. We then introduced the AuNP-corona formed from each individual protein into an acidic solution at pH 6.2 with high ionic concentration for up to 24 h to examine for changes in their aggregation in a cancer microenvironment model. We observed that protein corona formation sterically stabilized the AuNP-corona for all four proteins, resulting in a smaller increase in aggregation and size compared to citrate-capped AuNPs. This was especially true for coronas formed at high protein:AuNP ratios. Our study therefore showed that the formation of a complete “corona coat” around NPs at sufficiently high protein:NP ratio was required for colloidal stability of designed NP systems in both physiological and cancer microenvironment to maintain efficiency and efficacy in cancer drug delivery.
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