An in-depth view of human serum albumin corona on gold nanoparticles

Abstract

Upon entering biological systems, such as the blood stream, nanoparticles form molecular complexes with the proteins encountered called protein coronas, which shield the surface of the exogenous nanoparticle. The most abundant blood proteins, such as albumin, initially occupy the surface of the nanoparticle. Owing to the widespread applications of gold nanoparticles in medicine, in this study, the docking of human serum albumin to gold nanoparticles was examined and the changes in protein structure were investigated by a molecular dynamic simulation and GOLP force field. The results showed that after the adsorption of albumin on the gold nanoparticle, human serum albumin was denatured and the amount of alpha-helix significantly decreased. Domain III, which has a large cavity of fatty acids binding sites, plays an important role in the adsorption on the gold nanoparticles. Lys464, Thr504, Phe505, and Leu581 are critical amino acids in HSA adsorption on the GNPs. After the adsorption of albumin on the surface of gold nanoparticles, the fluctuations in some of the domains of the protein increased. Variations in the helix properties, such as helix length, dipole, radius, average phi and psi angles, and the length of hydrogen bonds, were calculated in detail.

Nanoparticle Ligand Exchange and Its Effects at the Nanoparticle–Cell Membrane Interface

“…For AuNP-S-Tn (which possess a desorption enthapy corresponding to alkanethiols of about 167 kJ mol -1 ), 37 ssDNA strands can "tie" tightly to the surface of AuNPs with a high density, which markedly enhances the affinity and coverage, and thereby inhibits ligand exchange ( Figure 4d); 3) For BSA-stabilized AuNPs, it had previously been found that BSA can be adsorbed onto the surface of AuNPs and form a rigid corona. Although the desorption energy of BSA from AuNPs was estimated to be only in the range of several tens of kJ/mol, 38,39 the large volume of BSA significantly improved the thickness of the ligand layer, preventing ligand exchange ( Figure S5g). Thus, a simplified two- (Figure 5b, c).…”

Quantitative Comparison of Protein Adsorption and Conformational Changes on Dielectric-Coated Nanoplasmonic Sensing Arrays

“…Understanding protein adsorption behavior on silica and titania surfaces is important considering their prevalence in biomedical applications [ 44 , 45 ]. HSA was selected as the model protein because it is widely studied and known to denature (via conformational changes) in the adsorbed state [ 46 , 47 , 48 , 49 , 50 ]. HSA is also a structural cognate of BSA [ 51 , 52 ], and this similarity provided the basis for comparing LSPR measurement data with past findings as further verification.…”

Targeting Ability of Affibody-Functionalized Particles Is Enhanced by Albumin but Inhibited by Serum Coronas

“…12,13 In particular, HSA has been used in fundamental studies of protein coronas formed on surfaces of nano-particles, because it is present in the corona of virtually all nanoparticles studied. [14][15][16] Although these studies provide important insights into how HSA interacts with nanoparticles, how well they reflect what occurs in more complex biological environments (e.g., in serum, or in blood plasma) has not been extensively explored. The aim of this study was to systematically compare the influence of protein coronas on the properties of functionalized polymer particles, especially their targeting abilities, by using the single model protein, HSA, and the more biologically relevant HS, a widely used in vitro model.…”