Control of surface tension at liquid-liquid interfaces using nanoparticles and nanoparticle-protein complexes

Langmuir. 2012 Jan 31;28(4):2023-7. doi: 10.1021/la204017z. Epub 2011 Dec 22.

Abstract

Subtle changes in the monolayer structure of nanoparticles (NPs) influence the interfacial behavior of both NPs and NP-protein conjugates. In this study, we use a series of monolayer-protected gold NPs to explore the role of particle hydrophobicity on their dynamic behavior at the toluene-water interface. Using dynamic surface tension measurements, we observed a linear decrease in the meso-equilibrium surface tension (γ) and faster dynamics as the hydrophobicity of the ligands increases. Further modulation of γ is observed for the corresponding NP-protein complexes at the charge-neutralization point.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Diffusion
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Ligands
  • Nanoparticles / chemistry*
  • Proteins / chemistry*
  • Surface Tension
  • Toluene / chemistry

Substances

  • Ligands
  • Proteins
  • Toluene