Shape dependent protein induced stabilization of gold nanoparticles: from protein corona perspective.

Abstract

Gold nanoparticles (GNPs) are promising materials for many bioapplications. However, upon contacting with biological media, GNPs undergo changes. The interaction with proteins results in the so-called protein corona (PC) around GNPs, leading to the new bioidentity and optical properties. Understanding the mechanisms of PC formation and its functions can help us to utilise its benefits and avoid its drawbacks. To date, most of the previous works aimed to understand the mechanisms governing PC formation and focused on the spherical nanoparticles although non-spherical nanoparticles are designed for a wide range of applications in biosensing. In this work, we investigated the differences in PC formation on spherical and anisotropic GNPs (nanostars in particular) from the joint experimental (extinction spectroscopy, zeta potential and surface enhanced Raman scattering [SERS]) and computational methods (the finite element method and molecular dynamics [MD] simulations). We discovered that protein does not fully cover the surface of anisotropic nanoparticles, leaving SERS hot-spots at the tips and high curvature edges “available” for analyte binding (no SERS signal after pre-incubation with protein) while providing protein-induced stabilization (indicated by extinction spectroscopy) of the GNPs by providing a protein layer around the particle’s core. The findings are confirmed from our MD simulations, the adsorption energy significantly decreases with the increased radius of curvature, so that tips (adsorption energy: 2762.334 kJ/mol) would be the least preferential binding site compared to core (adsorption energy: 11819.263 kJ/mol). These observations will help the development of new nanostructures with improved sensing and targeting ability.