ao9b03716_si_001.pdf (551.58 kB)
Comparative Analysis of Au and Au@SiO2 Nanoparticle–Protein Interactions for Evaluation as Platforms in Theranostic Applications
journal contribution
posted on 2020-03-20, 17:49 authored by Derrick J. Swinton, Hongxia Zhang, Arezue F. B. Boroujerdi, Keyana L. Tyree, Ricardo A. Burke, Makayla F. Turner, Imrana H. Salia, Tekiah S. McClaryGold
nanoparticles are utilized in a variety of sensing and detection
technologies because of their unique physiochemical properties. Their
tunable size, shape, and surface charge enable them to be used in
an array of platforms. The purpose of this study is to conduct a thorough
spectroscopic characterization of Au and functionalized hybrid Au@SiO2 nanoparticles under physiological conditions and in the presence
of two proteins known to be abundant in serum, bovine serum albumin
and human ubiquitin. The information obtained from this study will
enable us to develop design principles to synthesize an array of surface-enhanced
Raman spectroscopy-based nanoparticles as platforms for theranostic
applications. We are particularly interested in tailoring the surface
chemistry of the Au@SiO2 nanoparticles for applications
in theranostic technologies. We employ common spectroscopic techniques,
with particular emphasis on circular dichroism and heteronuclear single
quantum correlation nuclear magnetic resonance (HSQC NMR) spectroscopy,
as combinatorial tools to understand protein conformational dynamics,
binding site interactions, and protein corona for the design of nanoparticles
capable of reaching their intended target in vivo. Our results conclude
that protein adsorption onto the nanoparticle surface prevents nanoparticle
aggregation. We observed that varying the ionic strength and type
of ion influences the aggregation and aggregation rate of each respective
nanoparticle. The conformation of proteins and the absorption of proteins
on the surface of Au nanoparticles are also influenced by ionic strength.
Using two-dimensional [15N–1H]-HSQC NMR
experiments to compare the interactions of Au and Au@SiO2 nanoparticles with 15N-ubiquitin, we observed small chemical
shift perturbations in some amino acid peaks and differences in binding
site interactions with ubiquitin and respective nanoparticles.
History
Usage metrics
Categories
Keywords
protein coronananoparticle aggregationsurface chemistrydetection technologiesHSQC NMRcombinatorial toolsComparative Analysisspectroscopic techniquessurface chargespectroscopic characterizationbinding site interactionsTheranostic Applications Gold nanoparticlesaggregation ratechemical shift perturbationsquantum correlation15 N-ubiquitintheranostic applicationsnanoparticle surfaceacid peaksion influencestheranostic technologiessurface-enhanced Raman spectroscopy-based nanoparticlesdesign principlestunable sizeprotein adsorptionserum albumin
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC