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Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels
Polyelectrolyte gels are useful as carriers of proteins and other biomacromolecules in, e.g., drug delivery. The rational design of such systems requires knowledge about how the binding and release are affected by electrostatic and hydrophobic interactions between the components. To this end we have...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318605/ https://www.ncbi.nlm.nih.gov/pubmed/30674786 http://dx.doi.org/10.3390/gels4010009 |
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author | Andersson, Martin Hansson, Per |
author_facet | Andersson, Martin Hansson, Per |
author_sort | Andersson, Martin |
collection | PubMed |
description | Polyelectrolyte gels are useful as carriers of proteins and other biomacromolecules in, e.g., drug delivery. The rational design of such systems requires knowledge about how the binding and release are affected by electrostatic and hydrophobic interactions between the components. To this end we have investigated the uptake of lysozyme by weakly crosslinked spherical poly(styrenesulfonate) (PSS) microgels and macrogels by means of micromanipulator assisted light microscopy and small angle X-ray scattering (SAXS) in an aqueous environment. The results show that the binding process is an order of magnitude slower than for cytochrome c and for lysozyme binding to sodium polyacrylate gels under the same conditions. This is attributed to the formation of very dense protein-rich shells in the outer layers of the microgels with low permeability to the protein. The shells in macrogels contain 60 wt % water and nearly charge stoichiometric amounts of lysozyme and PSS in the form of dense complexes of radius 8 nm comprising 30–60 lysozyme molecules. With support from kinetic modelling results we propose that the rate of protein binding and the relaxation rate of the microgel are controlled by the protein mass transport through the shell, which is strongly affected by hydrophobic and electrostatic interactions. The mechanism explains, in turn, an observed dependence of the diffusion rate on the apparent degree of crosslinking of the networks. |
format | Online Article Text |
id | pubmed-6318605 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63186052019-01-17 Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels Andersson, Martin Hansson, Per Gels Article Polyelectrolyte gels are useful as carriers of proteins and other biomacromolecules in, e.g., drug delivery. The rational design of such systems requires knowledge about how the binding and release are affected by electrostatic and hydrophobic interactions between the components. To this end we have investigated the uptake of lysozyme by weakly crosslinked spherical poly(styrenesulfonate) (PSS) microgels and macrogels by means of micromanipulator assisted light microscopy and small angle X-ray scattering (SAXS) in an aqueous environment. The results show that the binding process is an order of magnitude slower than for cytochrome c and for lysozyme binding to sodium polyacrylate gels under the same conditions. This is attributed to the formation of very dense protein-rich shells in the outer layers of the microgels with low permeability to the protein. The shells in macrogels contain 60 wt % water and nearly charge stoichiometric amounts of lysozyme and PSS in the form of dense complexes of radius 8 nm comprising 30–60 lysozyme molecules. With support from kinetic modelling results we propose that the rate of protein binding and the relaxation rate of the microgel are controlled by the protein mass transport through the shell, which is strongly affected by hydrophobic and electrostatic interactions. The mechanism explains, in turn, an observed dependence of the diffusion rate on the apparent degree of crosslinking of the networks. MDPI 2018-01-16 /pmc/articles/PMC6318605/ /pubmed/30674786 http://dx.doi.org/10.3390/gels4010009 Text en © 2018 by the authors. 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/). |
spellingShingle | Article Andersson, Martin Hansson, Per Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title | Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title_full | Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title_fullStr | Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title_full_unstemmed | Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title_short | Binding of Lysozyme to Spherical Poly(styrenesulfonate) Gels |
title_sort | binding of lysozyme to spherical poly(styrenesulfonate) gels |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318605/ https://www.ncbi.nlm.nih.gov/pubmed/30674786 http://dx.doi.org/10.3390/gels4010009 |
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