4.6 Article

Adsorption of a Protein Mono layer via Hydrophobic Interactions Prevents Nanoparticle Aggregation under Harsh Environmental Conditions

Journal

ACS SUSTAINABLE CHEMISTRY & ENGINEERING
Volume 1, Issue 7, Pages 833-842

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/sc400042h

Keywords

Gold nanoparticles; Surface plasmon; Bovine serum albumin; Protein corona; Correlation spectroscopy; Diffusion

Funding

  1. Robert A. Welch Foundation [C-1664, C-1787]
  2. Cancer Prevention and Research Institute of Texas [CPRIT RP110355]
  3. ARO MUM [W911NF-12-1-0407]
  4. National Science Foundation [CBET-1134417, CHE-1151647]
  5. National Institutes of Health [GM94246-01A1]
  6. National Science Foundation through a Graduate Research Fellowship [0940902]

Ask authors/readers for more resources

We find that citrate-stabilized gold nanoparticles aggregate and precipitate in saline solutions below the NaCl concentration of many bodily fluids and blood plasma. Our experiments indicate that this is due to complexation of the citrate anions with Na+ cations in solution. A dramatically enhanced colloidal stability is achieved when bovine serum albumin is adsorbed to the gold nanoparticle surface, completely preventing nanoparticle aggregation under harsh environmental conditions where the NaCl concentration is well beyond the isotonic point. Furthermore, we explore the mechanism of the formation of this albumin corona and find that monolayer protein adsorption is most likely ruled by hydrophobic interactions. As for many nanotechnology-based biomedical and environmental applications, particle aggregation and sedimentation are undesirable and could substantially increase the risk of toxicological side effects; the formation of the BSA corona presented here provides a low-cost biocompatible strategy for nanoparticle stabilization and transport in highly ionic environments.

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