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Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry

[Image: see text] Core–shell nanoparticles receive much attention for their current and potential applications in life sciences. Commonly, a dense shell of hydrated polymer, a polymer brush, is grafted to improve colloidal stability of functional nanoparticles and to prevent protein adsorption, aggr...

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Autores principales: Gal, Noga, Schroffenegger, Martina, Reimhult, Erik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5994724/
https://www.ncbi.nlm.nih.gov/pubmed/29726682
http://dx.doi.org/10.1021/acs.jpcb.8b02338
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author Gal, Noga
Schroffenegger, Martina
Reimhult, Erik
author_facet Gal, Noga
Schroffenegger, Martina
Reimhult, Erik
author_sort Gal, Noga
collection PubMed
description [Image: see text] Core–shell nanoparticles receive much attention for their current and potential applications in life sciences. Commonly, a dense shell of hydrated polymer, a polymer brush, is grafted to improve colloidal stability of functional nanoparticles and to prevent protein adsorption, aggregation, cell recognition, and uptake. Until recently, it was widely assumed that a polymer brush shell indeed prevents strong association of proteins and that this leads to their superior “stealth” properties in vitro and in vivo. We show using T-dependent isothermal titration calorimetry on well-characterized monodisperse superparamagnetic iron oxide nanoparticles with controlled dense stealth polymer brush shells that “stealth” core–shell nanoparticles display significant attractive exothermic and enthalpic interactions with serum proteins, despite having excellent colloidal stability and negligible nonspecific cell uptake. This observation is at room temperature shown to depend only weakly on variation of iron oxide core diameter and type of grafted stealth polymer: poly(ethylene glycol), poly(ethyl oxazoline), poly(isopropyl oxazoline), and poly(N-isopropyl acrylamide). Polymer brush shells with a critical solution temperature close to body temperature showed a strong temperature dependence in their interactions with proteins with a significant increase in protein binding energy with increased temperature. The stoichiometry of interaction is estimated to be near 1:1 for PEGylated nanoparticles and up to 10:1 for larger thermoresponsive nanoparticles, whereas the average free energy of interaction is enthalpically driven and comparable to a weak hydrogen bond.
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spelling pubmed-59947242018-06-12 Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry Gal, Noga Schroffenegger, Martina Reimhult, Erik J Phys Chem B [Image: see text] Core–shell nanoparticles receive much attention for their current and potential applications in life sciences. Commonly, a dense shell of hydrated polymer, a polymer brush, is grafted to improve colloidal stability of functional nanoparticles and to prevent protein adsorption, aggregation, cell recognition, and uptake. Until recently, it was widely assumed that a polymer brush shell indeed prevents strong association of proteins and that this leads to their superior “stealth” properties in vitro and in vivo. We show using T-dependent isothermal titration calorimetry on well-characterized monodisperse superparamagnetic iron oxide nanoparticles with controlled dense stealth polymer brush shells that “stealth” core–shell nanoparticles display significant attractive exothermic and enthalpic interactions with serum proteins, despite having excellent colloidal stability and negligible nonspecific cell uptake. This observation is at room temperature shown to depend only weakly on variation of iron oxide core diameter and type of grafted stealth polymer: poly(ethylene glycol), poly(ethyl oxazoline), poly(isopropyl oxazoline), and poly(N-isopropyl acrylamide). Polymer brush shells with a critical solution temperature close to body temperature showed a strong temperature dependence in their interactions with proteins with a significant increase in protein binding energy with increased temperature. The stoichiometry of interaction is estimated to be near 1:1 for PEGylated nanoparticles and up to 10:1 for larger thermoresponsive nanoparticles, whereas the average free energy of interaction is enthalpically driven and comparable to a weak hydrogen bond. American Chemical Society 2018-05-04 2018-06-07 /pmc/articles/PMC5994724/ /pubmed/29726682 http://dx.doi.org/10.1021/acs.jpcb.8b02338 Text en Copyright © 2018 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 Gal, Noga
Schroffenegger, Martina
Reimhult, Erik
Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title_full Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title_fullStr Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title_full_unstemmed Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title_short Stealth Nanoparticles Grafted with Dense Polymer Brushes Display Adsorption of Serum Protein Investigated by Isothermal Titration Calorimetry
title_sort stealth nanoparticles grafted with dense polymer brushes display adsorption of serum protein investigated by isothermal titration calorimetry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5994724/
https://www.ncbi.nlm.nih.gov/pubmed/29726682
http://dx.doi.org/10.1021/acs.jpcb.8b02338
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