Development of Dye Ligands and Dye Affinity Adsorbents

The originally exploited dyes were commercial textile chlorotriazine aromatic polysulfonated molecules

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which when attached to appropriate supports, usually bearing hydroxyl groups, yield dye affinity adsorbents. The range of shades of commercial dyes derives primarily from anthraquinone, azo and phthalocyanine chromophores bonded to suitable reactive functions such as triazinyl and other mainly polyhalogenated heterocyclics. Anthraquinone dyes produce blue and the phthalocyanines turquoise shades. Green dyes contain mixed anthraquinone-stilbene, anthraquinone-azo or phthalocyanine-azo structures, whereas most other shades are derived from the azo class.

Unlike most biological affinity adsorbents, the stability of dye affinity adsorbents is usually limited only by the support itself. Dyes offer clear advantages over biological ligands, in terms of economy, ease of immobilization, safety, stability and adsorbent capacity. The main drawback of textile dyes is their moderate selectivity during the protein-binding process. In spite of this, the overall size, shape and distribution of ionic and hydrophobic groups enable dyes to interact with the binding sites(s) of proteins sometimes fairly specifically, as for example, with the nucleotide-binding site of several dehydro-genases, kinases, and several nucleotide-recognizing enzymes. The dye-protein interaction should not be compared to a simple ion exchange type since binding is frequently possible at pHs greater than the pi of the targeted protein. Furthermore, dissociation of the dye-protein complex is often achieved specifically by competing ligands, suggesting interaction with the protein at discrete sites. The view is supported by chromatographic, kinetic, inactivation, affinity labelling and spectra difference studies.

The last few years have seen a novel approach for tackling the problem of dye selectivity, signalling the

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