Biomimetic dyes as affinity chromatography tools in enzyme purification

Citation
Yd. Clonis et al., Biomimetic dyes as affinity chromatography tools in enzyme purification, J CHROMAT A, 891(1), 2000, pp. 33-44
Citations number
27
Categorie Soggetti
Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences
Journal title
Volume
891
Issue
1
Year of publication
2000
Pages
33 - 44
Database
ISI
SICI code
Abstract
Affinity adsorbents based on immobilized triazine dyes offer important adva ntages circumventing many of the problems associated with biological ligand s. The main drawback of dyes is their moderate selectivity for proteins. Ra tional attempts to tackle this problem are realized through the biomimetic dye concept according to which new dyes, the biomimetic dyes, are designed to mimic natural ligands. Biomimetic dyes are expected to exhibit increased affinity and purifying ability for the targeted proteins. Biocomputing off ers a powerful approach to biomimetic ligand design. The successful exploit ation of contemporary computational techniques in molecular design requires the knowledge of the three-dimensional structure of the target protein, or at least, the amino acid sequence of the target protein and the three-dime nsional structure of a highly homologous protein. From such information one can then design, on a graphics workstation, the model of the protein and a lso a number of suitable synthetic ligands which mimic natural biological l igands of the protein. There are several examples of enzyme purifications ( trypsin, urokinase, kallikrein, alkaline phosphatase, malate dehydrogenase, formate dehydrogenase, oxaloacetate decarboxylase and lactate dehydrogenas e) where synthetic biomimetic dyes have been used successfully as affinity chromatography tools. (C) 2000 Elsevier Science B.V. All rights reserved.