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Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles

[Image: see text] The adsorption of proteins from aqueous medium leads to the formation of protein corona on nanoparticles. The formation of protein corona is governed by a complex interplay of protein–particle and protein–protein interactions, such as electrostatics, van der Waals, hydrophobic, hyd...

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Autores principales: Lee, Jin Gyun, Lannigan, Kelly, Shelton, William A., Meissner, Jens, Bharti, Bhuvnesh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7735741/
https://www.ncbi.nlm.nih.gov/pubmed/33210541
http://dx.doi.org/10.1021/acs.langmuir.0c01613
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author Lee, Jin Gyun
Lannigan, Kelly
Shelton, William A.
Meissner, Jens
Bharti, Bhuvnesh
author_facet Lee, Jin Gyun
Lannigan, Kelly
Shelton, William A.
Meissner, Jens
Bharti, Bhuvnesh
author_sort Lee, Jin Gyun
collection PubMed
description [Image: see text] The adsorption of proteins from aqueous medium leads to the formation of protein corona on nanoparticles. The formation of protein corona is governed by a complex interplay of protein–particle and protein–protein interactions, such as electrostatics, van der Waals, hydrophobic, hydrogen bonding, and solvation. The experimental parameters influencing these interactions, and thus governing the protein corona formation on nanoparticles, are currently poorly understood. This lack of understanding is due to the complexity in the surface charge distribution and anisotropic shape of the protein molecules. Here, we investigate the effect of pH and salinity on the characteristics of corona formed by myoglobin on silica nanoparticles. We experimentally measure and theoretically model the adsorption isotherms of myoglobin binding to silica nanoparticles. By combining adsorption studies with surface electrostatic mapping of myoglobin, we demonstrate that a monolayered hard corona is formed in low salinity dispersions, which transforms into a multilayered hard + soft corona upon the addition of salt. We attribute the observed changes in protein adsorption behavior with increasing pH and salinity to the change in electrostatic interactions and surface charge regulation effects. This study provides insights into the mechanism of protein adsorption and corona formation on nanoparticles, which would guide future studies on optimizing nanoparticle design for maximum functional benefits and minimum toxicity.
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spelling pubmed-77357412020-12-15 Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles Lee, Jin Gyun Lannigan, Kelly Shelton, William A. Meissner, Jens Bharti, Bhuvnesh Langmuir [Image: see text] The adsorption of proteins from aqueous medium leads to the formation of protein corona on nanoparticles. The formation of protein corona is governed by a complex interplay of protein–particle and protein–protein interactions, such as electrostatics, van der Waals, hydrophobic, hydrogen bonding, and solvation. The experimental parameters influencing these interactions, and thus governing the protein corona formation on nanoparticles, are currently poorly understood. This lack of understanding is due to the complexity in the surface charge distribution and anisotropic shape of the protein molecules. Here, we investigate the effect of pH and salinity on the characteristics of corona formed by myoglobin on silica nanoparticles. We experimentally measure and theoretically model the adsorption isotherms of myoglobin binding to silica nanoparticles. By combining adsorption studies with surface electrostatic mapping of myoglobin, we demonstrate that a monolayered hard corona is formed in low salinity dispersions, which transforms into a multilayered hard + soft corona upon the addition of salt. We attribute the observed changes in protein adsorption behavior with increasing pH and salinity to the change in electrostatic interactions and surface charge regulation effects. This study provides insights into the mechanism of protein adsorption and corona formation on nanoparticles, which would guide future studies on optimizing nanoparticle design for maximum functional benefits and minimum toxicity. American Chemical Society 2020-11-19 2020-12-01 /pmc/articles/PMC7735741/ /pubmed/33210541 http://dx.doi.org/10.1021/acs.langmuir.0c01613 Text en © 2020 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
spellingShingle Lee, Jin Gyun
Lannigan, Kelly
Shelton, William A.
Meissner, Jens
Bharti, Bhuvnesh
Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title_full Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title_fullStr Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title_full_unstemmed Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title_short Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
title_sort adsorption of myoglobin and corona formation on silica nanoparticles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7735741/
https://www.ncbi.nlm.nih.gov/pubmed/33210541
http://dx.doi.org/10.1021/acs.langmuir.0c01613
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