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. 2019 Jun 25;4(6):11044-11052.
doi: 10.1021/acsomega.9b01240. eCollection 2019 Jun 30.

Assembly of Multicomponent Nano-Bioconjugates Composed of Mesoporous Silica Nanoparticles, Proteins, and Gold Nanoparticles

Giulia Rossella Delpiano  1 , Maria F Casula  1 , Marco Piludu  2 , Riccardo Corpino  2 , Pier Carlo Ricci  2 , María Vallet-Regí  3 , Enrico Sanjust  2 , Maura Monduzzi  1 , Andrea Salis  1
Affiliations

Assembly of Multicomponent Nano-Bioconjugates Composed of Mesoporous Silica Nanoparticles, Proteins, and Gold Nanoparticles

Giulia Rossella Delpiano et al. ACS Omega. .

Abstract

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-NH2) were synthesized and characterized through various techniques (small angle X-rays scattering TEM, N2 adsorption/desorption isotherms, and thermogravimetric analysis (TGA)). BSA or lysozyme were then grafted on the external surface of MSN-NH2 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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Conflict of interest statement

The authors declare no competing financial interest.

Figures

Scheme 1
Scheme 1. Assembly of the MSN–Protein–GNP Nano-Bioconjugates
The MSN surface is functionalized with aminopropyltriethoxysilane (APTES) to obtain MSN–NH2. Proteins (BSA or lysozyme) are grafted, by means of glutaraldehyde, on the external surface of MSN–NH2 to obtain MSN–protein bioconjugates. The MSN–protein samples are dispersed in a gold nanoparticle (GNP) solution to obtain MSN–protein–GNPs nano-bioconjugates. TEM images show the occurrence of GNPs on the MSN–protein surface, whereas almost no GNPs occur in the protein-free control samples.
Figure 1
Figure 1
Characterization of MSN–NH2 by (A) TEM, (B) SAXS, (C) N2-physisorption isotherm, and (D) pore size distribution.
Figure 2
Figure 2
Thermogravimetric analysis. Mass loss (%) profiles as a function of the temperature of MSN–NH2, MSN–GA, MSN–LYZ, and MSN–BSA samples.
Figure 3
Figure 3
TEM images of (a–f) MSN–BSA and (a′–f′) MSN–LYZ treated with GNPs. Control sample (protein-free) images are shown in Figure S2 (Supporting Information).
Figure 4
Figure 4
TEM images of MSN–NH2 (protein-free) particles loaded with 5 nm (top) and 20 nm (bottom) GNP.
Figure 5
Figure 5
Fluorescence spectra of (A) BSA/GNPs and (B) LYZ/GNPs aqueous solutions with different volume ratios. (C) Raman spectrum of LYZ/GNPs conjugate solution.
Figure 6
Figure 6
Structure of BSA (PDB file: 3V03) and lysozyme (PDB file: 1LYZ). Tryptophan residues are colored in red. Images obtained with visual molecular dynamics software.
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