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Temperature: the "ignored" factor at the nanobio interface

Mahmoudi, M ; Sharif University of Technology | 2013

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  1. Type of Document: Article
  2. DOI: 10.1021/nn305337c
  3. Publisher: 2013
  4. Abstract:
  5. Upon incorporation of nanoparticles (NPs) into the body, they are exposed to biological fluids, and their interaction with the dissolved biomolecules leads to the formation of the so-called protein corona on the surface of the NPs. The composition of the corona plays a crucial role in the biological fate of the NPs. While the effects of various physicochemical parameters on the composition of the corona have been explored in depth, the role of temperature upon its formation has received much less attention. In this work, we have probed the effect of temperature on the protein composition on the surface of a set of NPs with various surface chemistries and electric charges. Our results indicate that the degree of protein coverage and the composition of the adsorbed proteins on the NPs' surface depend on the temperature at which the protein corona is formed. Also, the uptake of NPs is affected by the temperature. Temperature is, thus, an important parameter that needs to be carefully controlled in quantitative studies of bionano interactions
  6. Keywords:
  7. Colloidal magnetic nanoparticles ; Protein corona ; Temperature dependence ; Uptake by cells ; Bionano-interactions ; Effect of temperature ; Magnetic nano-particles ; Physicochemical parameters ; Protein adsorption ; Protein composition ; Protein coronas ; Molecular biology ; Nanoparticles ; Surface chemistry ; Proteins ; Nanoparticle ; polymer ; Protein ; Serum albumin ; Colloid ; Biotechnology ; Chemistry ; Confocal microscopy ; HeLa cell ; Human ; Kinetics ; Magnetism ; PH ; Surface property ; Temperature ; Transmission electron microscopy ; HeLa cell line ; Magnetics ; Mass Spectrometry ; Microscopy, Confocal ; Microscopy, Electron, Transmission ; Adsorption ; Colloids ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Particle Size ; Polymers ; Protein Binding
  8. Source: ACS Nano ; Volume 7, Issue 8 , 2013 , Pages 6555-6562 ; 19360851 (ISSN)
  9. URL: http://pubs.acs.org/doi/abs/10.1021/nn305337c