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Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies

Albumin-based cryogels for capturing haemin were synthesised by crosslinking different biomolecules, bovine serum albumin (BSA) and ovalbumin (OVA). The impact of the protein and coupling agent concentrations on cryogel’s mechanical properties, swelling ratios and polymerisation yields, as well as a...

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Autores principales: Hajizadeh, Solmaz, Dicko, Cedric, Bülow, Leif
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742477/
https://www.ncbi.nlm.nih.gov/pubmed/36518195
http://dx.doi.org/10.3389/fbioe.2022.1072153
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author Hajizadeh, Solmaz
Dicko, Cedric
Bülow, Leif
author_facet Hajizadeh, Solmaz
Dicko, Cedric
Bülow, Leif
author_sort Hajizadeh, Solmaz
collection PubMed
description Albumin-based cryogels for capturing haemin were synthesised by crosslinking different biomolecules, bovine serum albumin (BSA) and ovalbumin (OVA). The impact of the protein and coupling agent concentrations on cryogel’s mechanical properties, swelling ratios and polymerisation yields, as well as autoclaving as a post-treatment on the cryogel, were studied. We found that BSA (50 mg/ml) and the crosslinker (N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride, 46 mg/ml) formed a cryogel with optimum physical characteristics at a comparatively low protein concentration. The cryogel’s mechanical stability was increased using a double-layer cryogel approach by crosslinking the BSA proteins at subzero temperature inside an acrylamide and hydroxyethyl methacrylate premade cryogels. Batch binding and kinetic adsorption isotherms of haemin on the cryogels were assessed to evaluate their binding capacity toward the porphyrin molecule. The results showed that single-layer cryogels (BSA and OVA) had a higher capacity (∼0.68 mg/ml gel) and higher reaction rate constant towards haemin adsorption than double-layer gels. In contrast, the double-layer cryogels had higher mechanical strength than single-layer gels. The experimental results suggested that the cryogels followed the Freundlich model and the pseudo-second-order isotherm for batch adsorption and kinetics, respectively. The interaction between haemin and the gels was studied by fluorescence quenching. We found between 1.1 and 1.6 binding sites for different cryogels.
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spelling pubmed-97424772022-12-13 Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies Hajizadeh, Solmaz Dicko, Cedric Bülow, Leif Front Bioeng Biotechnol Bioengineering and Biotechnology Albumin-based cryogels for capturing haemin were synthesised by crosslinking different biomolecules, bovine serum albumin (BSA) and ovalbumin (OVA). The impact of the protein and coupling agent concentrations on cryogel’s mechanical properties, swelling ratios and polymerisation yields, as well as autoclaving as a post-treatment on the cryogel, were studied. We found that BSA (50 mg/ml) and the crosslinker (N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride, 46 mg/ml) formed a cryogel with optimum physical characteristics at a comparatively low protein concentration. The cryogel’s mechanical stability was increased using a double-layer cryogel approach by crosslinking the BSA proteins at subzero temperature inside an acrylamide and hydroxyethyl methacrylate premade cryogels. Batch binding and kinetic adsorption isotherms of haemin on the cryogels were assessed to evaluate their binding capacity toward the porphyrin molecule. The results showed that single-layer cryogels (BSA and OVA) had a higher capacity (∼0.68 mg/ml gel) and higher reaction rate constant towards haemin adsorption than double-layer gels. In contrast, the double-layer cryogels had higher mechanical strength than single-layer gels. The experimental results suggested that the cryogels followed the Freundlich model and the pseudo-second-order isotherm for batch adsorption and kinetics, respectively. The interaction between haemin and the gels was studied by fluorescence quenching. We found between 1.1 and 1.6 binding sites for different cryogels. Frontiers Media S.A. 2022-11-28 /pmc/articles/PMC9742477/ /pubmed/36518195 http://dx.doi.org/10.3389/fbioe.2022.1072153 Text en Copyright © 2022 Hajizadeh, Dicko and Bülow. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Hajizadeh, Solmaz
Dicko, Cedric
Bülow, Leif
Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title_full Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title_fullStr Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title_full_unstemmed Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title_short Interaction of haemin with albumin-based macroporous cryogel: Adsorption isotherm and fluorescence quenching studies
title_sort interaction of haemin with albumin-based macroporous cryogel: adsorption isotherm and fluorescence quenching studies
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742477/
https://www.ncbi.nlm.nih.gov/pubmed/36518195
http://dx.doi.org/10.3389/fbioe.2022.1072153
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