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.
Highlights
Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(v-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applications
I n a recent study[1] protein-like, partially reversible associative behaviour was observed in solutions of the water soluble class of carbohydrates known as the 6-deoxy-6-(v-aminoalkyl)aminocelluloses[2]
As we found with other 6-deoxy-6-(v-aminoalkyl)aminocelluloses[1], the technique of sedimentation velocity in the analytical ultracentrifuge revealed several components present: the components sedimenting above 1 Svedberg (S 5 10213 sec, the same unit which is traditionally used, for example, to classify ribosome sizes) follow a step-wise series rule for globular macromolecules: si varies as i2/3, where i is the peak number
Summary
Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(v-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applications. I n a recent study[1] protein-like, partially reversible associative behaviour was observed in solutions of the water soluble class of carbohydrates known as the 6-deoxy-6-(v-aminoalkyl)aminocelluloses[2] These molecules provide controllable self-assembling films for enzyme immobilisation and other biotechnological applications[2] and are a class of cellulose based carbohydrate polymer which have been rendered aqueous soluble by substitution at the C-6 carbon with a particular amino chain (Fig. 1a). The powerful analytical methods of sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge[3] were used to demonstrate and evaluate the oligomeric nature of the preparation[4,5] These methods – highly successful in the study of oligomeric behavior of proteins provide separation of species of different molecular mass without the need for any separation media – as required by chromatographic or membrane based procedures, and are not affected by supramolecular contamination as in light scattering based procedures. Once formed these carbohydrate tetramers are seen to associate further in a regular way into larger supra-molecular complexes
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