Spatial Mapping and Quantification of Soft and Hard Protein Coronas at Silver Nanocubes

Abstract

Protein coronas around silver nanocubes were quantified in serum-containing media using localized surface plasmon resonances. Both soft and hard coronas showed exposure-time and concentration-dependent changes in protein surface density with time-dependent hardening. We observed spatially dependent kinetics of the corona-formation at cube edges/corners versus facets at short incubation times, where the polymer stabilization agent delayed corona hardening. The soft corona contained more protein than the hard corona at all time-points (8-fold difference with 10% serum conditions).

Effect of the protein corona on nanoparticles for modulating cytotoxicity and immunotoxicity

“…[36][37][38] Recently, protein coronas adsorbed on polyvinylpyrrolidone-stabilized silver nanocubes in fetal bovine serum (FBS)-containing media were also quantified, using localized surface plasmon resonances. 32 The soft corona formation was identified at the cube edges/corners versus facets at short incubation times. 32 The soft corona also contained more proteins than the hard corona at all points (eightfold difference in 10% serum condition; Figure 6).…”

“…32 The soft corona formation was identified at the cube edges/corners versus facets at short incubation times. 32 The soft corona also contained more proteins than the hard corona at all points (eightfold difference in 10% serum condition; Figure 6). 32 This study suggests that polymer-coated NP coating may influence the kinetics of corona formation or protein distribution on NPs in biological media.…”

“…[26][27][28][29][30][31][32] [33][34][35] For example, Roach et al studied the binding events of bovine serum albumin (BSA) and bovine fibrinogen (BFG) on silica nanospheres that exhibited both hydrophilic and hydrophobic surface curvature and performed secondary structure analysis (ie, infrared spectroscopy on surface-bound proteins). 35 Compared with BSA, fibrinogen tended to undergo greater conformational changes in its secondary structure when proteins were adsorbed on NPs with high surface curvature (ie, small dimension of radius).…”

“…In addition, the plasma-derived hard corona (ie, the final long-term corona) may be important when NPs are accumulated in various organs. 9,20,54 Adhesion to hydrophobicity 35 Molecular weight 25,32 Endosome-Lysosome trafficking 13,21 Conformational changes (sheet) 35 Cedervall et al determined that the kinetic and equilibrium binding properties of NP-protein coronas depend not only on the NP surface and size but also on plasma protein identity, such as with HSA, fibrinogen, and lipoproteins. 24 For example, HSA and fibrinogen exhibited higher rates of association and dissociation than apolipoprotein A-I and other plasma proteins.…”

Silver nanoparticle-induced hemoglobin decrease involves alteration of histone 3 methylation status

“…1B), indicating that AgNPs were well dispersed in culture medium. The slight increase of hydrodynamic size should be due to the formation of protein corona on AgNPs [39,40]. The zeta-potential analysis showed that AgNPs were negatively charged in culture medium over the time course (Fig.…”