ABSTRACT
Affinity chromatography is likely to play an increasingly important role in the purification of pharmaceutical proteins. This review describes new approaches to the design and synthesis of affinity ligands based on the ability to combine knowledge of X-ray crystallographic or NMR structures with defined or combinatorial chemical synthesis. The de novo design process is based on peptidal templates, complementarity to surface exposed residues and mimicking natural biological recognition. Examples of ligands designed to bind specifically to kallikrein, elastase, immunoglobulin G, insulin, alpha(1)-antitrypsin, clotting factor VII and glyco-proteins are given. The exceptional selectivity and stability of these synthetic ligands allows their use in harsh manufacturing environments.
Subject(s)
Biopharmaceutics/methods , Chromatography, Affinity/methods , Chromatography, Affinity/trends , Combinatorial Chemistry Techniques , Crystallography, X-Ray/methods , Drug Design , Ligands , Magnetic Resonance SpectroscopyABSTRACT
In this survey, score analyses of 123 male and female respondents, ages 21 to 33 years, yielded no significant differences between either sex and smokers versus nonsmokers on Rotter's locus of control scale. Of particular interest was that nonpracticing smokers (quitters) scored more internal than either smokers or nonsmokers.
