Studies at the nanoparticle-biomolecular interface and beyond
type: CreativeWork
description: Gold nanoparticles (Au NPs) have attracted much interest in biological applications due to their excellent optoelectronic properties and ease of surface functionalization. However, while Au NPs are positioned to revolutionize nanotechnology based biomedical applications, our fundamental understanding at the nanoparticle-biomolecular interface and its resultant impact on cells is still limited. In particular, analysis of the spatial arrangement of nanoparticle’s surface ligands using scanning tunneling microscopy is a highly controversial topic. Addition of nanoparticles to cell culture media was shown to result in a hard and soft protein corona formation, which acted to mitigate/reduce the proposed chemical capabilities of nanoparticles. More critically but even less well understood is the precise orientation of proteins upon adsorption as well as the possible change in protein’s conformation, which can alter the protein’s intrinsic function. This dissertation will thus focus on developing our understanding at this interface, by probing the chemistries at this nanoparticle-biomolecular interface and subsequently, how the Au NPs influence cellular responses. The question of spatial location of different ligands on nanoparticle surfaces with diameters less than 100 nm is an important one that is difficult to quantitatively address. To investigate the spatial arrangement of biomolecules on Au NPs, the surface of 20, 50, and 90 nm Au NPs were functionalized with two different lipids, both single and mixed, using two different surface chemical procedures utilizing electrostatic or hydrophobic interactions. Mass spectrometry supported the presence of both lipids in the mixed-lipid systems on nanoparticles, and it was observed that the surface chemistry of Au NPs influenced the relative ratios of mixed lipids incorporated. Electron microscopy evidence showed domain sizes for one lipid apparently a quarter to a half the projected diameter for 50 and 90 nm particles; but for…
abstract: Gold nanoparticles (Au NPs) have attracted much interest in biological applications due to their excellent optoelectronic properties and ease of surface functionalization. However, while Au NPs are positioned to revolutionize nanotechnology based biomedical applications, our fundamental understanding at the nanoparticle-biomolecular interface and its resultant impact on cells is still limited. In particular, analysis of the spatial arrangement of nanoparticle’s surface ligands using scanning tunneling microscopy is a highly controversial topic. Addition of nanoparticles to cell culture media was shown to result in a hard and soft protein corona formation, which acted to mitigate/reduce the proposed chemical capabilities of nanoparticles. More critically but even less well understood is the precise orientation of proteins upon adsorption as well as the possible change in protein’s conformation, which can alter the protein’s intrinsic function. This dissertation will thus focus on developing our understanding at this interface, by probing the chemistries at this nanoparticle-biomolecular interface and subsequently, how the Au NPs influence cellular responses. The question of spatial location of different ligands on nanoparticle surfaces with diameters less than 100 nm is an important one that is difficult to quantitatively address. To investigate the spatial arrangement of biomolecules on Au NPs, the surface of 20, 50, and 90 nm Au NPs were functionalized with two different lipids, both single and mixed, using two different surface chemical procedures utilizing electrostatic or hydrophobic interactions. Mass spectrometry supported the presence of both lipids in the mixed-lipid systems on nanoparticles, and it was observed that the surface chemistry of Au NPs influenced the relative ratios of mixed lipids incorporated. Electron microscopy evidence showed domain sizes for one lipid apparently a quarter to a half the projected diameter for 50 and 90 nm particles; but for…
author: Yang, Jie An
language: en
keywords: Gold nanoparticles, lipid adsorption, alpha synuclein, protein adsorption, protein orientation, cell migration, gene expression
date published: 2014-01-16T18:24:52Z
date modified: 2026-07-22T22:25:38Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/46876