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Título:
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Assembly of Multicomponent Nano-Bioconjugates Composed ofMesoporous Silica Nanoparticles, Proteins, and Gold Nanoparticles
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Autores:
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Delpiano, Giulia ;
Casula, Maria ;
Piludu, Marco ;
Corpino, Riccardo ;
Ricci, Pier Carlo ;
Vallet Regí, María ;
Sanjust, Enrico ;
Monduzzi, Maura ;
Salis, Andrea
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Tipo de documento:
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texto impreso
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Editorial:
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American Chemical Society, 2019-06-25
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Dimensiones:
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application/pdf
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Nota general:
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cc_by_nc_nd
info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias: Química: Materiales
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Materia = Ciencias Biomédicas: Farmacia: Química inorgánica
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Tipo = Artículo
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Resumen:
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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 nanobioconjugates 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, ?-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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En línea:
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https://eprints.ucm.es/id/eprint/56154/1/Accepted%20manuscript.pdf
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