Publication: Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: A comprehensive quantitative proteomic analysis
0
0
Issued Date
2011
Resource Type
File Type
application/pdf
ISSN
19360851
Other identifier(s)
2-s2.0-80053328840
Rights Holder(s)
Scopus
Bibliographic Citation
ACS Nano. Vol 5, No.9 (2011), p.7155-7167
Suggested Citation
Tenzer S., Docter D., Rosfa S., Wlodarski A., Kuharev J., Rekik A., Knauer S.K., Bantz C., Nawroth T., Bier C., Sirirattanapan J., Mann W., Treuel L., Zellner R., Maskos M., Schild H., Stauber R.H. Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: A comprehensive quantitative proteomic analysis. ACS Nano. Vol 5, No.9 (2011), p.7155-7167. doi:10.1021/nn201950e Retrieved from: https://hdl.handle.net/20.500.14740/7239
Abstract
In biological fluids, proteins associate with nanoparticles, leading to a protein "corona" defining the biological identity of the particle. However, a comprehensive knowledge of particle-guided protein fingerprints and their dependence on nanomaterial properties is incomplete. We studied the long-lived ("hard") blood plasma derived corona on monodispersed amorphous silica nanoparticles differing in size (20, 30, and 100 nm). Employing label-free liquid chromatography mass spectrometry, one- and two-dimensional gel electrophoresis, and immunoblotting the composition of the protein corona was analyzed not only qualitatively but also quantitatively. Detected proteins were bioinformatically classified according to their physicochemical and biological properties. Binding of the 125 identified proteins did not simply reflect their relative abundance in the plasma but revealed an enrichment of specific lipoproteins as well as proteins involved in coagulation and the complement pathway. In contrast, immunoglobulins and acute phase response proteins displayed a lower affinity for the particles. Protein decoration of the negatively charged particles did not correlate with protein size or charge, demonstrating that electrostatic effects alone are not the major driving force regulating the nanoparticle-protein interaction. Remarkably, even differences in particle size of only 10 nm significantly determined the nanoparticle corona, although no clear correlation with particle surface volume, protein size, or charge was evident. Particle size quantitatively influenced the particle's decoration with 37% of all identified proteins, including (patho)biologically relevant candidates. We demonstrate the complexity of the plasma corona and its still unresolved physicochemical regulation, which need to be considered in nanobioscience in the future. © 2011 American Chemical Society.
Subject(s)
Bionanoscience
Colloidal chemistry
Liquid chromatography mass spectrometry
Nanomedicines
Nanotoxicity
Bioinformatics
Blood
Coagulation
Electrophoresis
Immunology
Liquid chromatography
Liquids
Mass spectrometry
Medical nanotechnology
Nanoparticles
Particle size analysis
Plasmas
Silica
Proteins
Nanoparticle
Article
Human
Mass spectrometry
Particle size
Plasma
Proteomics
Humans
Mass Spectrometry
Nanoparticles
Particle Size
Plasma
Proteomics
Colloidal chemistry
Liquid chromatography mass spectrometry
Nanomedicines
Nanotoxicity
Bioinformatics
Blood
Coagulation
Electrophoresis
Immunology
Liquid chromatography
Liquids
Mass spectrometry
Medical nanotechnology
Nanoparticles
Particle size analysis
Plasmas
Silica
Proteins
Nanoparticle
Article
Human
Mass spectrometry
Particle size
Plasma
Proteomics
Humans
Mass Spectrometry
Nanoparticles
Particle Size
Plasma
Proteomics