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Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability
In the natural fluidic environment of a biological system, nanoparticles swiftly adsorb plasma proteins on their surface forming a “protein corona”, which profoundly and often adversely affects their residence in the systemic circulation in vivo and their interaction with cells in vitro. It has been...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8037850/ https://www.ncbi.nlm.nih.gov/pubmed/33800633 http://dx.doi.org/10.3390/ma14071657 |
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author | Shanwar, Samah Liang, Liuen Nechaev, Andrey V. Bausheva, Daria K. Balalaeva, Irina V. Vodeneev, Vladimir A. Roy, Indrajit Zvyagin, Andrei V. Guryev, Evgenii L. |
author_facet | Shanwar, Samah Liang, Liuen Nechaev, Andrey V. Bausheva, Daria K. Balalaeva, Irina V. Vodeneev, Vladimir A. Roy, Indrajit Zvyagin, Andrei V. Guryev, Evgenii L. |
author_sort | Shanwar, Samah |
collection | PubMed |
description | In the natural fluidic environment of a biological system, nanoparticles swiftly adsorb plasma proteins on their surface forming a “protein corona”, which profoundly and often adversely affects their residence in the systemic circulation in vivo and their interaction with cells in vitro. It has been recognized that preformation of a protein corona under controlled conditions ameliorates the protein corona effects, including colloidal stability in serum solutions. We report on the investigation of the stabilizing effects of a denatured bovine serum albumin (dBSA) protein corona formed on the surface of upconversion nanoparticles (UCNPs). UCNPs were chosen as a nanoparticle model due to their unique photoluminescent properties suitable for background-free biological imaging and sensing. UCNP surface was modified with nitrosonium tetrafluoroborate (NOBF(4)) to render it hydrophilic. UCNP-NOBF(4) nanoparticles were incubated in dBSA solution to form a dBSA corona followed up by lyophilization. As produced dBSA-UCNP-NOBF(4) demonstrated high photoluminescence brightness, sustained colloidal stability after long-term storage and the reduced level of serum protein surface adsorption. These results show promise of dBSA-based nanoparticle pretreatment to improve the amiability to biological environments towards theranostic applications. |
format | Online Article Text |
id | pubmed-8037850 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80378502021-04-12 Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability Shanwar, Samah Liang, Liuen Nechaev, Andrey V. Bausheva, Daria K. Balalaeva, Irina V. Vodeneev, Vladimir A. Roy, Indrajit Zvyagin, Andrei V. Guryev, Evgenii L. Materials (Basel) Article In the natural fluidic environment of a biological system, nanoparticles swiftly adsorb plasma proteins on their surface forming a “protein corona”, which profoundly and often adversely affects their residence in the systemic circulation in vivo and their interaction with cells in vitro. It has been recognized that preformation of a protein corona under controlled conditions ameliorates the protein corona effects, including colloidal stability in serum solutions. We report on the investigation of the stabilizing effects of a denatured bovine serum albumin (dBSA) protein corona formed on the surface of upconversion nanoparticles (UCNPs). UCNPs were chosen as a nanoparticle model due to their unique photoluminescent properties suitable for background-free biological imaging and sensing. UCNP surface was modified with nitrosonium tetrafluoroborate (NOBF(4)) to render it hydrophilic. UCNP-NOBF(4) nanoparticles were incubated in dBSA solution to form a dBSA corona followed up by lyophilization. As produced dBSA-UCNP-NOBF(4) demonstrated high photoluminescence brightness, sustained colloidal stability after long-term storage and the reduced level of serum protein surface adsorption. These results show promise of dBSA-based nanoparticle pretreatment to improve the amiability to biological environments towards theranostic applications. MDPI 2021-03-28 /pmc/articles/PMC8037850/ /pubmed/33800633 http://dx.doi.org/10.3390/ma14071657 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Shanwar, Samah Liang, Liuen Nechaev, Andrey V. Bausheva, Daria K. Balalaeva, Irina V. Vodeneev, Vladimir A. Roy, Indrajit Zvyagin, Andrei V. Guryev, Evgenii L. Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title | Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title_full | Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title_fullStr | Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title_full_unstemmed | Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title_short | Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability |
title_sort | controlled formation of a protein corona composed of denatured bsa on upconversion nanoparticles improves their colloidal stability |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8037850/ https://www.ncbi.nlm.nih.gov/pubmed/33800633 http://dx.doi.org/10.3390/ma14071657 |
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