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Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †

Human serum albumin (HSA) is one of the most frequently immobilized proteins on the surface of carriers, including magnetic nanoparticles. This is because the drug–HSA interaction study is one of the basic pharmacokinetic parameters determined for drugs. In spite of many works describing the immobil...

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Autores principales: Ziegler-Borowska, Marta, Mylkie, Kinga, Kozlowska, Mariana, Nowak, Pawel, Chelminiak-Dudkiewicz, Dorota, Kozakiewicz, Anna, Ilnicka, Anna, Kaczmarek-Kedziera, Anna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572529/
https://www.ncbi.nlm.nih.gov/pubmed/31109114
http://dx.doi.org/10.3390/molecules24101925
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author Ziegler-Borowska, Marta
Mylkie, Kinga
Kozlowska, Mariana
Nowak, Pawel
Chelminiak-Dudkiewicz, Dorota
Kozakiewicz, Anna
Ilnicka, Anna
Kaczmarek-Kedziera, Anna
author_facet Ziegler-Borowska, Marta
Mylkie, Kinga
Kozlowska, Mariana
Nowak, Pawel
Chelminiak-Dudkiewicz, Dorota
Kozakiewicz, Anna
Ilnicka, Anna
Kaczmarek-Kedziera, Anna
author_sort Ziegler-Borowska, Marta
collection PubMed
description Human serum albumin (HSA) is one of the most frequently immobilized proteins on the surface of carriers, including magnetic nanoparticles. This is because the drug–HSA interaction study is one of the basic pharmacokinetic parameters determined for drugs. In spite of many works describing the immobilization of HSA and the binding of active substances, research describing the influence of the used support on the effectiveness of immobilization is missing. There are also no reports about the effect of the support drying method on the effectiveness of protein immobilization. This paper examines the effect of both the method of functionalizing the polymer coating covering magnetic nanoparticles (MNPs), and the drying methods for the immobilization of HSA. Albumin was immobilized on three types of aminated chitosan-coated nanoparticles with a different content of amino groups long distanced from the surface Fe(3)O(4)-CS-Et(NH(2))(1–3). The obtained results showed that both the synthesis method and the method of drying nanoparticles have a large impact on the effectiveness of immobilization. Due to the fact that the results obtained for Fe(3)O(4)-CS-Et(NH(2))(2) significantly differ from those obtained for the others, the influence of the geometry of the shell structure on the ability to bind HSA was also explained by molecular dynamics.
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spelling pubmed-65725292019-06-18 Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization † Ziegler-Borowska, Marta Mylkie, Kinga Kozlowska, Mariana Nowak, Pawel Chelminiak-Dudkiewicz, Dorota Kozakiewicz, Anna Ilnicka, Anna Kaczmarek-Kedziera, Anna Molecules Article Human serum albumin (HSA) is one of the most frequently immobilized proteins on the surface of carriers, including magnetic nanoparticles. This is because the drug–HSA interaction study is one of the basic pharmacokinetic parameters determined for drugs. In spite of many works describing the immobilization of HSA and the binding of active substances, research describing the influence of the used support on the effectiveness of immobilization is missing. There are also no reports about the effect of the support drying method on the effectiveness of protein immobilization. This paper examines the effect of both the method of functionalizing the polymer coating covering magnetic nanoparticles (MNPs), and the drying methods for the immobilization of HSA. Albumin was immobilized on three types of aminated chitosan-coated nanoparticles with a different content of amino groups long distanced from the surface Fe(3)O(4)-CS-Et(NH(2))(1–3). The obtained results showed that both the synthesis method and the method of drying nanoparticles have a large impact on the effectiveness of immobilization. Due to the fact that the results obtained for Fe(3)O(4)-CS-Et(NH(2))(2) significantly differ from those obtained for the others, the influence of the geometry of the shell structure on the ability to bind HSA was also explained by molecular dynamics. MDPI 2019-05-18 /pmc/articles/PMC6572529/ /pubmed/31109114 http://dx.doi.org/10.3390/molecules24101925 Text en © 2019 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
Ziegler-Borowska, Marta
Mylkie, Kinga
Kozlowska, Mariana
Nowak, Pawel
Chelminiak-Dudkiewicz, Dorota
Kozakiewicz, Anna
Ilnicka, Anna
Kaczmarek-Kedziera, Anna
Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title_full Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title_fullStr Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title_full_unstemmed Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title_short Effect of Geometrical Structure, Drying, and Synthetic Method on Aminated Chitosan-Coated Magnetic Nanoparticles Utility for HSA Effective Immobilization †
title_sort effect of geometrical structure, drying, and synthetic method on aminated chitosan-coated magnetic nanoparticles utility for hsa effective immobilization †
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572529/
https://www.ncbi.nlm.nih.gov/pubmed/31109114
http://dx.doi.org/10.3390/molecules24101925
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