Journal of Chromatography B, Volume 790, Issues 1-2 , 25 June 2003, Pages 67-78
Preparative Chromatography of Proteins
N. E. Labrou
Laboratory of Enzyme Technology, Department of Agricultural Biotechnology, Agricultural University of Athens, 75 Iera Odos Street, GR-11855, Athens, Greece
Available online 20 May 2003.
Abstract
Affinity chromatography is potentially the most selective method for protein purification. The technique has the purification power to eliminate steps, increase yields and thereby improve process economics. However, it suffers from problems regarding ligand stability and cost. Some of the most recent advances in this area have explored the power of rational and combinatorial approaches for designing highly selective and stable synthetic affinity ligands. Rational molecular design techniques, which are based on the ability to combine knowledge of protein structures with defined chemical synthesis and advanced computational tools, have made rational ligand design feasible and faster. Combinatorial approaches based on peptide and nucleic acid libraries have permitted the rapid synthesis of new synthetic affinity ligands of potential use in affinity chromatography. The versatility of these approaches suggests that, in the near future, they will become the dominant methods for designing and selection of novel affinity ligands with scale-up potential.
Author Keywords: Proteins; Peptides
Subject-index terms: Reviews; Combinatorial design; Ligand design; Molecular docking; Phage display; Ribosome display; Systematic evolution of ligand by exponential enrichment; Affinity adsorbents
Corresponding author. Tel./fax: +30-210-529-4308. | 
