Adsorbed Proteins Influence the Biological Activity and Molecular Targeting of Nanomaterials

Abstract

The possible combination of specific physicochemical properties operating at unique sites of action within cells and tissues has led to considerable uncertainty surrounding nanomaterial toxic potential. We have investigated the importance of proteins adsorbed onto the surface of two distinct classes of nanomaterials (single-walled carbon nanotubes [SWCNTs]; 10-nm amorphous silica) in guiding nanomaterial uptake or toxicity in the RAW 264.7 macrophage-like model. Albumin was identified as the major fetal bovine or human serum/plasma protein adsorbed onto SWCNTs, while a distinct protein adsorption profile was observed when plasma from the Nagase analbuminemic rat was used. Damaged or structurally altered albumin is rapidly cleared from systemic circulation by scavenger receptors. We observed that SWCNTs inhibited the induction of cyclooxygenase-2 (Cox-2) by lipopolysaccharide (LPS; 1 ng/ml, 6 h) and this anti-inflammatory response was inhibited by fucoidan (scavenger receptor antagonist). Fucoidan also reduced the uptake of fluorescent SWCNTs (Alexa647). Precoating SWCNTs with a nonionic surfactant (Pluronic F127) inhibited albumin adsorption and anti-inflammatory properties. Albumin-coated SWCNTs reduced LPS-mediated Cox-2 induction under serum-free conditions. SWCNTs did not reduce binding of LPS(Alexa488) to RAW 264.7 cells. The profile of proteins adsorbed onto amorphous silica particles (50-1000 nm) was qualitatively different, relative to SWCNTs, and precoating amorphous silica with Pluronic F127 dramatically reduced the adsorption of serum proteins and toxicity. Collectively, these observations suggest an important role for adsorbed proteins in modulating the uptake and toxicity of SWCNTs and nano-sized amorphous silica.

The intensity of internalization and cytotoxicity of superparamagnetic iron oxide nanoparticles with different surface modifications in human tumor and diploid lung cells

“…These data indicated that MNPs internalization might affect also the ratio between the serum proteins and the amount of nanoparticles. The protein corona has been shown to be a dynamic structure, largely determined by the extracellular milieu [35,36], and substantially influences dispersion, biodistribution, mechanism of internalization and biological activity of nanoparticles [33,37]. Albumin, fibrinogen and immunoglobulins (Ig) have been shown to be the principal plasma proteins that bind to iron oxide nanoparticles when they come in contact with plasma [38].…”

Effect of Silica Surface Properties on the Formation of Multilayer or Submonolayer Protein Hard Corona: Albumin Adsorption on Pyrolytic and Colloidal SiO2 Nanoparticles

“…In one study, it was also found to be the most abundant protein in the hard corona of silica NPs, 59 while in other cases, its content in the hard protein corona was very low. [60][61][62] Physical parameters such as the surface curvature of NPs were proposed to play a role in the competitive adsorption of proteins in the process, resulting in the formation of the hard corona. 22 It could be of interest to investigate the possible contribution of different amounts and distributions of surface silanols to the composition of the hard protein corona on SiO 2 NPs.…”

The on-bead digestion of protein corona on nanoparticles by trypsin immobilized on the magnetic nanoparticle

“…As reported previously, the protein corona on nanoparticles would critically impact the biological identities of nanoparticles [6][7][8][9] and/or result in the physiological and pathological consequences of the macrophage uptake, blood coagulation, complement activation and cellular toxicity, etc. [10][11][12][13][14][15][16]. The elaborate investigation on protein corona would accordingly make great sense for the extensive application of nanomaterials.…”