ArticleScientific reports2014
Protein-like fully reversible tetramerisation and super-association of an aminocellulose.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Comparative sedimentation equilibrium analysis of two IgG1 glycoforms: IgGCri and IgGWid.European biophysics journal : EBJ · 2023Article
- A functional bimodal mesoporous silica nanoparticle with redox/cellulase dual-responsive gatekeepers for controlled release of fungicide.Scientific reports · 2023Article
- Article
- Analytical Ultracentrifugation as a Matrix-Free Probe for the Study of Kinase Related Cellular and Bacterial Membrane Proteins and Glycans.Molecules (Basel, Switzerland) · 2021Review
- Aminoethyl substitution enhances the self-assembly properties of an aminocellulose as a potential archaeological wood consolidant.European biophysics journal : EBJ · 2020Article
- Characterisation of the molecular properties of scleroglucan as an alternative rigid rod molecule to xanthan gum for oropharyngeal dysphagia.Food hydrocolloids · 2020Article
- The Svedberg Lecture 2017. From nano to micro: the huge dynamic range of the analytical ultracentrifuge for characterising the sizes, shapes and interactions of molecules and assemblies in Biochemistry and Polymer Science.European biophysics journal : EBJ · 2018Article
- Full hydrodynamic reversibility of the weak dimerization of vancomycin and elucidation of its interaction with VanS monomers at clinical concentration.Scientific reports · 2017Article
- Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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