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Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae
Fucoidans are a diverse class of sulfated polysaccharides integral to the cell wall of brown algae, and due to their various bioactivities, they are potential drugs. Standardized work with fucoidans is required for structure–function studies, but remains challenging since available fucoidan preparat...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8091464/ https://www.ncbi.nlm.nih.gov/pubmed/32651947 http://dx.doi.org/10.1093/glycob/cwaa064 |
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author | Sichert, Andreas Le Gall, Sophie Klau, Leesa Jane Laillet, Brigitte Rogniaux, Hélène Aachmann, Finn Lillelund Hehemann, Jan-Hendrik |
author_facet | Sichert, Andreas Le Gall, Sophie Klau, Leesa Jane Laillet, Brigitte Rogniaux, Hélène Aachmann, Finn Lillelund Hehemann, Jan-Hendrik |
author_sort | Sichert, Andreas |
collection | PubMed |
description | Fucoidans are a diverse class of sulfated polysaccharides integral to the cell wall of brown algae, and due to their various bioactivities, they are potential drugs. Standardized work with fucoidans is required for structure–function studies, but remains challenging since available fucoidan preparations are often contaminated with other algal compounds. Additionally, fucoidans are structurally diverse depending on species and season, urging the need for standardized purification protocols. Here, we use ion-exchange chromatography to purify different fucoidans and found a high structural diversity between fucoidans. Ion-exchange chromatography efficiently removes the polysaccharides alginate and laminarin and other contaminants such as proteins and phlorotannins across a broad range of fucoidans from major brown algal orders including Ectocarpales, Laminariales and Fucales. By monomer composition, linkage analysis and NMR characterization, we identified galacturonic acid, glucuronic acid and O-acetylation as new structural features of certain fucoidans and provided a novel structure of fucoidan from Durvillaea potatorum with α-1,3-linked fucose backbone and β-1,6 and β-1,3 galactose branches. This study emphasizes the use of standardized ion-exchange chromatography to obtain defined fucoidans for subsequent molecular studies. |
format | Online Article Text |
id | pubmed-8091464 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-80914642021-05-12 Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae Sichert, Andreas Le Gall, Sophie Klau, Leesa Jane Laillet, Brigitte Rogniaux, Hélène Aachmann, Finn Lillelund Hehemann, Jan-Hendrik Glycobiology Analytical Glycobiology Fucoidans are a diverse class of sulfated polysaccharides integral to the cell wall of brown algae, and due to their various bioactivities, they are potential drugs. Standardized work with fucoidans is required for structure–function studies, but remains challenging since available fucoidan preparations are often contaminated with other algal compounds. Additionally, fucoidans are structurally diverse depending on species and season, urging the need for standardized purification protocols. Here, we use ion-exchange chromatography to purify different fucoidans and found a high structural diversity between fucoidans. Ion-exchange chromatography efficiently removes the polysaccharides alginate and laminarin and other contaminants such as proteins and phlorotannins across a broad range of fucoidans from major brown algal orders including Ectocarpales, Laminariales and Fucales. By monomer composition, linkage analysis and NMR characterization, we identified galacturonic acid, glucuronic acid and O-acetylation as new structural features of certain fucoidans and provided a novel structure of fucoidan from Durvillaea potatorum with α-1,3-linked fucose backbone and β-1,6 and β-1,3 galactose branches. This study emphasizes the use of standardized ion-exchange chromatography to obtain defined fucoidans for subsequent molecular studies. Oxford University Press 2020-07-11 /pmc/articles/PMC8091464/ /pubmed/32651947 http://dx.doi.org/10.1093/glycob/cwaa064 Text en © The Author(s) 2020. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Analytical Glycobiology Sichert, Andreas Le Gall, Sophie Klau, Leesa Jane Laillet, Brigitte Rogniaux, Hélène Aachmann, Finn Lillelund Hehemann, Jan-Hendrik Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title | Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title_full | Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title_fullStr | Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title_full_unstemmed | Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title_short | Ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
title_sort | ion-exchange purification and structural characterization of five sulfated fucoidans from brown algae |
topic | Analytical Glycobiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8091464/ https://www.ncbi.nlm.nih.gov/pubmed/32651947 http://dx.doi.org/10.1093/glycob/cwaa064 |
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