Cargando…
Protein–like fully reversible tetramerisation and super-association of an aminocellulose
Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(ω-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applicat...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3900928/ https://www.ncbi.nlm.nih.gov/pubmed/24457430 http://dx.doi.org/10.1038/srep03861 |
_version_ | 1782300782887960576 |
---|---|
author | Nikolajski, Melanie Adams, Gary G. Gillis, Richard B. Besong, David Tabot Rowe, Arthur J. Heinze, Thomas Harding, Stephen E. |
author_facet | Nikolajski, Melanie Adams, Gary G. Gillis, Richard B. Besong, David Tabot Rowe, Arthur J. Heinze, Thomas Harding, Stephen E. |
author_sort | Nikolajski, Melanie |
collection | PubMed |
description | Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(ω-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applications. Now, for the first time, we have found a fully reversible self-association (tetramerisation) within this family of polysaccharides. Remarkably these carbohydrate tetramers are then seen to associate further in a regular way into supra-molecular complexes. Fully reversible oligomerisation has been hitherto completely unknown for carbohydrates and instead resembles in some respects the assembly of polypeptides and proteins like haemoglobin and its sickle cell mutation. Our traditional perceptions as to what might be considered “protein-like” and what might be considered as “carbohydrate-like” behaviour may need to be rendered more flexible, at least as far as interaction phenomena are concerned. |
format | Online Article Text |
id | pubmed-3900928 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-39009282014-01-24 Protein–like fully reversible tetramerisation and super-association of an aminocellulose Nikolajski, Melanie Adams, Gary G. Gillis, Richard B. Besong, David Tabot Rowe, Arthur J. Heinze, Thomas Harding, Stephen E. Sci Rep Article Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(ω-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applications. Now, for the first time, we have found a fully reversible self-association (tetramerisation) within this family of polysaccharides. Remarkably these carbohydrate tetramers are then seen to associate further in a regular way into supra-molecular complexes. Fully reversible oligomerisation has been hitherto completely unknown for carbohydrates and instead resembles in some respects the assembly of polypeptides and proteins like haemoglobin and its sickle cell mutation. Our traditional perceptions as to what might be considered “protein-like” and what might be considered as “carbohydrate-like” behaviour may need to be rendered more flexible, at least as far as interaction phenomena are concerned. Nature Publishing Group 2014-01-24 /pmc/articles/PMC3900928/ /pubmed/24457430 http://dx.doi.org/10.1038/srep03861 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Article Nikolajski, Melanie Adams, Gary G. Gillis, Richard B. Besong, David Tabot Rowe, Arthur J. Heinze, Thomas Harding, Stephen E. Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title | Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title_full | Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title_fullStr | Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title_full_unstemmed | Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title_short | Protein–like fully reversible tetramerisation and super-association of an aminocellulose |
title_sort | protein–like fully reversible tetramerisation and super-association of an aminocellulose |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3900928/ https://www.ncbi.nlm.nih.gov/pubmed/24457430 http://dx.doi.org/10.1038/srep03861 |
work_keys_str_mv | AT nikolajskimelanie proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT adamsgaryg proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT gillisrichardb proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT besongdavidtabot proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT rowearthurj proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT heinzethomas proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose AT hardingstephene proteinlikefullyreversibletetramerisationandsuperassociationofanaminocellulose |