title: Control of surface tension at liquid-liquid interfaces using nanoparticles and nanoparticle-protein complexes.
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.
authors.affiliation: Department of Chemistry, University of Massachusetts at Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
authors.forename: Subinoy
authors.initials: S
authors.lastname: Rana
authors.forename: Xi
authors.initials: X
authors.lastname: Yu
authors.forename: Debabrata
authors.initials: D
authors.lastname: Patra
authors.forename: Daniel F
authors.initials: DF
authors.lastname: Moyano
authors.forename: Oscar R
authors.initials: OR
authors.lastname: Miranda
authors.forename: Irshad
authors.initials: I
authors.lastname: Hussain
authors.forename: Vincent M
authors.initials: VM
authors.lastname: Rotello
mesh_terms: D004058:Diffusion; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008024:Ligands; D053758:Nanoparticles / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013500:Surface Tension; D014050:Toluene / Q000737:chemistry
chemical_list: D008024:Ligands; D011506:Proteins; D014050:Toluene