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Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5

ABSTRACT: The development of synthetic particles that emulate real viruses in size, shape, and chemical composition is vital to the development of imprinted polymer-based sorbent materials (molecularly imprinted polymers, MIPs). In this study, we address surrogates for adenovirus type 5 (Adv 5) via...

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Autores principales: Fresco-Cala, Beatriz, López-Lorente, Ángela I., Batista, Alex D., Dinc, Mehmet, Bansmann, Joachim, Behm, R. Jürgen, Cárdenas, Soledad, Mizaikoff, Boris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9589707/
https://www.ncbi.nlm.nih.gov/pubmed/36274111
http://dx.doi.org/10.1007/s00216-022-04368-x
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author Fresco-Cala, Beatriz
López-Lorente, Ángela I.
Batista, Alex D.
Dinc, Mehmet
Bansmann, Joachim
Behm, R. Jürgen
Cárdenas, Soledad
Mizaikoff, Boris
author_facet Fresco-Cala, Beatriz
López-Lorente, Ángela I.
Batista, Alex D.
Dinc, Mehmet
Bansmann, Joachim
Behm, R. Jürgen
Cárdenas, Soledad
Mizaikoff, Boris
author_sort Fresco-Cala, Beatriz
collection PubMed
description ABSTRACT: The development of synthetic particles that emulate real viruses in size, shape, and chemical composition is vital to the development of imprinted polymer-based sorbent materials (molecularly imprinted polymers, MIPs). In this study, we address surrogates for adenovirus type 5 (Adv 5) via the synthesis and subsequent modification of icosahedral gold nanoparticles (iAuNPs) decorated with the most abundant protein of the Adv 5 (i.e., hexon protein) at the surface. CTAB-capped iAuNPs with dimensions in the range of 40–90 nm were synthesized, and then CTAB was replaced by a variety of polyethylene glycols (PEGs) in order to introduce suitable functionalities serving as anchoring points for the attachment of the hexon protein. The latter was achieved by non-covalent linking of the protein to the iAuNP surface using a PEG without reactive termination (i.e., methoxy PEG thiol, mPEG-SH, Mn=800). Alternatively, covalent anchoring points were generated by modifying the iAuNPs with a bifunctional PEG (i.e., thiol PEG amine, SH-PEG-NH(2)) followed by the addition of glutaraldehyde. X-ray photoelectron spectroscopy (XPS) confirmed the formation of the anchoring points at the iAuNP surface. Next, the amino groups present in the amino acids of the hexon protein interacted with the glutaraldehyde. iAuNPs before and after PEGylation were characterized using dynamic light scattering (DLS), XPS, transmission electron microscopy (TEM), scanning electron microscopy (SEM), and UV–Vis spectroscopy, confirming the CTAB–PEG exchange. Finally, the distinct red shift obtained in the UV–Vis spectra of the pegylated iAuNPs in the presence of the hexon protein, the increase in the hydrodynamic diameter, the change in the zeta potential, and the selective binding of the hexon-modified iAuNPs towards a hexon-imprinted polymer (HIP) confirmed success in both the covalent and non-covalent attachment at the iAuNP surface. GRAPHICAL ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00216-022-04368-x.
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spelling pubmed-95897072022-10-24 Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5 Fresco-Cala, Beatriz López-Lorente, Ángela I. Batista, Alex D. Dinc, Mehmet Bansmann, Joachim Behm, R. Jürgen Cárdenas, Soledad Mizaikoff, Boris Anal Bioanal Chem Research Paper ABSTRACT: The development of synthetic particles that emulate real viruses in size, shape, and chemical composition is vital to the development of imprinted polymer-based sorbent materials (molecularly imprinted polymers, MIPs). In this study, we address surrogates for adenovirus type 5 (Adv 5) via the synthesis and subsequent modification of icosahedral gold nanoparticles (iAuNPs) decorated with the most abundant protein of the Adv 5 (i.e., hexon protein) at the surface. CTAB-capped iAuNPs with dimensions in the range of 40–90 nm were synthesized, and then CTAB was replaced by a variety of polyethylene glycols (PEGs) in order to introduce suitable functionalities serving as anchoring points for the attachment of the hexon protein. The latter was achieved by non-covalent linking of the protein to the iAuNP surface using a PEG without reactive termination (i.e., methoxy PEG thiol, mPEG-SH, Mn=800). Alternatively, covalent anchoring points were generated by modifying the iAuNPs with a bifunctional PEG (i.e., thiol PEG amine, SH-PEG-NH(2)) followed by the addition of glutaraldehyde. X-ray photoelectron spectroscopy (XPS) confirmed the formation of the anchoring points at the iAuNP surface. Next, the amino groups present in the amino acids of the hexon protein interacted with the glutaraldehyde. iAuNPs before and after PEGylation were characterized using dynamic light scattering (DLS), XPS, transmission electron microscopy (TEM), scanning electron microscopy (SEM), and UV–Vis spectroscopy, confirming the CTAB–PEG exchange. Finally, the distinct red shift obtained in the UV–Vis spectra of the pegylated iAuNPs in the presence of the hexon protein, the increase in the hydrodynamic diameter, the change in the zeta potential, and the selective binding of the hexon-modified iAuNPs towards a hexon-imprinted polymer (HIP) confirmed success in both the covalent and non-covalent attachment at the iAuNP surface. GRAPHICAL ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00216-022-04368-x. Springer Berlin Heidelberg 2022-10-24 2023 /pmc/articles/PMC9589707/ /pubmed/36274111 http://dx.doi.org/10.1007/s00216-022-04368-x Text en © Springer-Verlag GmbH Germany, part of Springer Nature 2022, Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Research Paper
Fresco-Cala, Beatriz
López-Lorente, Ángela I.
Batista, Alex D.
Dinc, Mehmet
Bansmann, Joachim
Behm, R. Jürgen
Cárdenas, Soledad
Mizaikoff, Boris
Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title_full Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title_fullStr Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title_full_unstemmed Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title_short Icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
title_sort icosahedral gold nanoparticles decorated with hexon protein: a surrogate for adenovirus serotype 5
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9589707/
https://www.ncbi.nlm.nih.gov/pubmed/36274111
http://dx.doi.org/10.1007/s00216-022-04368-x
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