Identification of serum proteins bound to industrial nanomaterials

• Published in: Toxicology letters Vol. 208; no. 1; pp. 41 - 50
• Main Authors: Ruh, Hermelindis, Kühl, Boris, Brenner-Weiss, Gerald, Hopf, Carsten, Diabaté, Silvia, Weiss, Carsten
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 05-01-2012; Elsevier
• Subjects: Albumin; Animals; Biological and medical sciences; Blood Proteins - analysis; Cattle; Chemical and industrial products toxicology. Toxic occupational diseases; Electrophoresis; Ferric Compounds - blood; Ferric Compounds - chemistry; Fibrinogen - analysis; Fibrinogen - chemistry; Humans; Immunoglobulin G - analysis; Immunoglobulin G - chemistry; In Vitro Techniques; Industrial nanomaterial; MALDI-TOF; Medical sciences; Metal oxide; Metals and various inorganic compounds; Nanoparticles - chemistry; Protein corona; Serum Albumin - analysis; Serum Albumin - chemistry; Serum protein; Silicon Dioxide - blood; Silicon Dioxide - chemistry; Soot - analysis; Soot - chemistry; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Surface Properties; Titanium - blood; Titanium - chemistry; Toxicology; Metal oxide; MALDI-TOF; Serum protein; Industrial nanomaterial; Protein corona; Oxides; Identification; Matrix assisted laser desorption ionization; Metal; Nanostructured materials
• ISSN: 0378-4274; 1879-3169
• DOI: 10.1016/j.toxlet.2011.09.009

► We studied the interaction of industrial nanomaterials with serum proteins. ► SiO
2, TiO
2, Fe
2O
3, and carbon black nanoparticles differently bind serum proteins. ► Different binding depends on the nanomaterial surface characteristics. ► Serum proteins bound to the nanomaterials were identified. ► Results will help to interpret results from
in vitro and
in vivo experiments.
Nanoparticles (NPs) are decorated with proteins and other biomolecules when they get into contact with biological systems. The presence of proteins in cell culture medium can therefore have effects on the biological outcome in cell-based tests. In this study, the manufactured nanomaterials silicon dioxide (SiO
2), titanium dioxide (TiO
2), iron-III-oxide (Fe
2O
3), and carbon black (CB) were used to study their interaction with single proteins from bovine and human plasma (albumin, fibrinogen and IgG) as well as with complete human serum. The protein binding capacity of the material was investigated and 1D gel electrophoresis was used to separate the bound proteins and to identify the bands by matrix-assisted laser desorption/ionisation-time-of-flight (MALDI-TOF) mass spectrometry.
We found that the NP surface chemistry had a great impact on the amount of bound protein with distinct ligands for each of the tested particles. The hydrophobic CB NPs bound much more protein than the hydrophilic metal oxide NPs. Among the single proteins investigated, fibrinogen showed the strongest affinity for SiO
2, TiO
2 and CB NPs. The identified proteins from human serum adsorbed to these NPs were very different. Only apolipoprotein A1 was found to be adsorbed to all NPs.
These studies will help to explain the different degree of biological responses observed after
in vitro exposure of cells in the absence or presence of serum and might also support the interpretation of
in vivo experiments were NPs come directly into contact with blood plasma.