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Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid
The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer’s disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions’ interactions with biological tissue and their interplay in Alzheimer’s...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9735935/ https://www.ncbi.nlm.nih.gov/pubmed/36500427 http://dx.doi.org/10.3390/molecules27238334 |
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author | Mahl, Cynthia Regina Albrecht Bataglioli, Rogério Aparecido Calais, Guilherme Bedeschi Taketa, Thiago Bezerra Beppu, Marisa Masumi |
author_facet | Mahl, Cynthia Regina Albrecht Bataglioli, Rogério Aparecido Calais, Guilherme Bedeschi Taketa, Thiago Bezerra Beppu, Marisa Masumi |
author_sort | Mahl, Cynthia Regina Albrecht |
collection | PubMed |
description | The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer’s disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions’ interactions with biological tissue and their interplay in Alzheimer’s disease. This work focuses on the role of the alginate composition on Cu(II) adsorption in the presence of histidine or β-amyloid, the peptide associated with the progression of Alzheimer’s disease. Alginate samples with different mannuronic/guluronic (M/G) ratios led to similar Cu(II) adsorption capacities, following the Langmuir isotherm and the pseudo-second-order adsorption kinetic models. Although the presence of histidine produced up to a 20% reduction in the copper adsorption capacity in guluronic-rich alginate samples (M/G~0.61), they presented stable bidentate chelation of the metallic ion. Chemical analyses (FTIR and XPS) demonstrated the role of hydroxyl and carboxyl groups in copper ion chelation, whereas both crystallinity and morphology analyses indicated the prevalence of histidine interaction with guluronic-rich alginate. Similar results were observed for Cu(II) adsorption in alginate beads in the presence of beta-amyloid and histidine, suggesting that the alginate/histidine system is a simple yet representative model to probe the application of biopolymers to metal ion uptake in the presence of biological competitors. |
format | Online Article Text |
id | pubmed-9735935 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97359352022-12-11 Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid Mahl, Cynthia Regina Albrecht Bataglioli, Rogério Aparecido Calais, Guilherme Bedeschi Taketa, Thiago Bezerra Beppu, Marisa Masumi Molecules Article The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer’s disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions’ interactions with biological tissue and their interplay in Alzheimer’s disease. This work focuses on the role of the alginate composition on Cu(II) adsorption in the presence of histidine or β-amyloid, the peptide associated with the progression of Alzheimer’s disease. Alginate samples with different mannuronic/guluronic (M/G) ratios led to similar Cu(II) adsorption capacities, following the Langmuir isotherm and the pseudo-second-order adsorption kinetic models. Although the presence of histidine produced up to a 20% reduction in the copper adsorption capacity in guluronic-rich alginate samples (M/G~0.61), they presented stable bidentate chelation of the metallic ion. Chemical analyses (FTIR and XPS) demonstrated the role of hydroxyl and carboxyl groups in copper ion chelation, whereas both crystallinity and morphology analyses indicated the prevalence of histidine interaction with guluronic-rich alginate. Similar results were observed for Cu(II) adsorption in alginate beads in the presence of beta-amyloid and histidine, suggesting that the alginate/histidine system is a simple yet representative model to probe the application of biopolymers to metal ion uptake in the presence of biological competitors. MDPI 2022-11-29 /pmc/articles/PMC9735935/ /pubmed/36500427 http://dx.doi.org/10.3390/molecules27238334 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Mahl, Cynthia Regina Albrecht Bataglioli, Rogério Aparecido Calais, Guilherme Bedeschi Taketa, Thiago Bezerra Beppu, Marisa Masumi Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title | Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title_full | Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title_fullStr | Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title_full_unstemmed | Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title_short | Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid |
title_sort | role of alginate composition on copper ion uptake in the presence of histidine or beta-amyloid |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9735935/ https://www.ncbi.nlm.nih.gov/pubmed/36500427 http://dx.doi.org/10.3390/molecules27238334 |
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