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.