Assembly of Multicomponent Nano-Bioconjugates Composed of Mesoporous Silica Nanoparticles, Proteins, and Gold Nanoparticles
Author(s) -
Giulia Rossella Delpiano,
Maria F. Casula,
Marco Piludu,
Riccardo Corpino,
Pier Carlo Ricci,
Maria ValletRegí,
Enrico Sanjust,
Maura Monduzzi,
Andrea Salis
Publication year - 2019
Publication title -
acs omega
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.9b01240
Subject(s) - bovine serum albumin , nanoparticle , mesoporous silica , colloidal gold , chemistry , nanomedicine , lysozyme , thermogravimetric analysis , mesoporous material , nanotechnology , protein adsorption , drug delivery , chemical engineering , materials science , adsorption , chromatography , organic chemistry , biochemistry , engineering , catalysis
The purpose of this work was the assembly of multicomponent nano-bioconjugates based on mesoporous silica nanoparticles (MSNs), proteins (bovine serum albumin, BSA, or lysozyme, LYZ), and gold nanoparticles (GNPs). These nano-bioconjugates may find applications in nanomedicine as theranostic devices. Indeed, MSNs can act as drug carriers, proteins stabilize MSNs within the bloodstream, or may have therapeutic or targeting functions. Finally, GNPs can either be used as contrast agents for imaging or for photothermal therapy. Here, amino-functionalized MSNs (MSN-NH 2 ) were synthesized and characterized through various techniques (small angle X-rays scattering TEM, N 2 adsorption/desorption isotherms, and thermogravimetric analysis (TGA)). BSA or lysozyme were then grafted on the external surface of MSN-NH 2 to obtain MSN-BSA and MSN-LYZ bioconjugates, respectively. Protein immobilization on MSNs surface was confirmed by Fourier transform infrared spectroscopy, ζ-potential measurements, and TGA, which also allowed the estimation of protein loading. The MSN-protein samples were then dispersed in a GNP solution to obtain MSN-protein-GNPs nano-bioconjugates. Transmission electron microscopy (TEM) analysis showed the occurrence of GNPs on the MSN-protein surface, whereas almost no GNPs occurred in the protein-free control samples. Fluorescence and Raman spectroscopies suggested that proteins-GNP interactions involve tryptophan residues.
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