Affinity chromatography matures as bioinformatic and combinatorial tools develop

dc.contributor.author	Clonis, YD	en
dc.date.accessioned	2014-06-06T06:46:58Z
dc.date.available	2014-06-06T06:46:58Z
dc.date.issued	2006	en
dc.identifier.issn	00219673	en
dc.identifier.uri	http://dx.doi.org/10.1016/j.chroma.2005.09.073	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/3330
dc.subject	Affinity chromatography	en
dc.subject	Affinity ligand	en
dc.subject	Bioinformatics	en
dc.subject	Combinatorial library	en
dc.subject	Dye-ligand	en
dc.subject	Enzyme purification	en
dc.subject	Ligand design	en
dc.subject	Microprotein scaffold	en
dc.subject	Protein purification	en
dc.subject	Proteomics	en
dc.subject	Rational design	en
dc.subject	Triazine scaffold	en
dc.subject.other	Affinity chromatography	en
dc.subject.other	Biotechnology	en
dc.subject.other	Drug products	en
dc.subject.other	Molecular structure	en
dc.subject.other	Proteins	en
dc.subject.other	Purification	en
dc.subject.other	Affinity ligand	en
dc.subject.other	Bioinformatics	en
dc.subject.other	Dye-ligand	en
dc.subject.other	Rational design	en
dc.subject.other	Liquid chromatography	en
dc.subject.other	alpha 1 antitrypsin	en
dc.subject.other	amino acid	en
dc.subject.other	amino acid derivative	en
dc.subject.other	antibody	en
dc.subject.other	carboxylic acid derivative	en
dc.subject.other	cellulose	en
dc.subject.other	chlorine derivative	en
dc.subject.other	galactose dehydrogenase	en
dc.subject.other	glucose oxidase	en
dc.subject.other	glycoprotein	en
dc.subject.other	heterocyclic compound	en
dc.subject.other	kallikrein	en
dc.subject.other	lactate dehydrogenase	en
dc.subject.other	ligand	en
dc.subject.other	oligonucleotide	en
dc.subject.other	oxoacid	en
dc.subject.other	peptide derivative	en
dc.subject.other	prion protein	en
dc.subject.other	protein	en
dc.subject.other	protein A	en
dc.subject.other	triazine	en
dc.subject.other	triazine derivative	en
dc.subject.other	affinity chromatography	en
dc.subject.other	bioinformatics	en
dc.subject.other	combinatorial library	en
dc.subject.other	liquid chromatography	en
dc.subject.other	phage display	en
dc.subject.other	priority journal	en
dc.subject.other	protein blood level	en
dc.subject.other	protein purification	en
dc.subject.other	protein structure	en
dc.subject.other	review	en
dc.subject.other	ribosome	en
dc.subject.other	synthesis	en
dc.subject.other	X ray crystallography	en
dc.subject.other	Aldehyde Oxidoreductases	en
dc.subject.other	alpha 1-Antitrypsin	en
dc.subject.other	Antibodies	en
dc.subject.other	Bacterial Proteins	en
dc.subject.other	Blood Coagulation Factors	en
dc.subject.other	Chromatography, Affinity	en
dc.subject.other	Coloring Agents	en
dc.subject.other	Combinatorial Chemistry Techniques	en
dc.subject.other	Computational Biology	en
dc.subject.other	DNA-Binding Proteins	en
dc.subject.other	Galactose Dehydrogenases	en
dc.subject.other	Glucose Oxidase	en
dc.subject.other	Glycoproteins	en
dc.subject.other	Kallikreins	en
dc.subject.other	L-Lactate Dehydrogenase	en
dc.subject.other	Ligands	en
dc.subject.other	Pancreatic Elastase	en
dc.subject.other	Peptide Library	en
dc.subject.other	Prions	en
dc.subject.other	Proinsulin	en
dc.subject.other	Protein Structure, Tertiary	en
dc.subject.other	Proteins	en
dc.subject.other	SELEX Aptamer Technique	en
dc.subject.other	Staphylococcal Protein A	en
dc.subject.other	Triazines	en
dc.title	Affinity chromatography matures as bioinformatic and combinatorial tools develop	en
heal.type	other	en
heal.identifier.primary	10.1016/j.chroma.2005.09.073	en
heal.publicationDate	2006	en
heal.abstract	Affinity chromatography has the reputation of a more expensive and less robust than other types of liquid chromatography. Furthermore, the technique is considered to stand a modest chance of large-scale purification of proteinaceous pharmaceuticals. This perception is changing because of the pressure for quality protein therapeutics, and the realization that higher returns can be expected when ensuring fewer purification steps and increased product recovery. These developments necessitated a rethinking of the protein purification processes and restored the interest for affinity chromatography. This liquid chromatography technique is designed to offer high specificity, being able to safely guide protein manufactures to successfully cope with the aforementioned challenges. Affinity ligands are distinguished into synthetic and biological. These can be generated by rational design or selected from ligand libraries. Synthetic ligands are generated by three methods. The rational method features the functional approach and the structural template approach. The combinatorial method relies on the selection of ligands from a library of synthetic ligands synthesized randomly. The combined method employs both methods, that is, the ligand is selected from an intentionally biased library based on a rationally designed ligand. Biological ligands are selected by employing high-throuphput biological techniques, e.g. phage- and ribosome-display for peptide and microprotein ligands, in addition to SELEX for oligonucleotide ligands. Synthetic mimodyes and chimaeric dye-ligands are usually designed by rational approaches and comprise a chloro-triazinlyl scaffold. The latter substituted with various amino acids, carbocyclic, and heterocyclic groups, generates libraries from which synthetic ligands can be selected. A 'lead' compound may help to generating a 'focused' or 'biased' library. This can be designed by various approaches, e.g.: (i) using a natural ligand-protein complex as a template; (ii) applying the principle of complementarity to exposed residues of the protein structure; and (iii) mimicking directly a natural biological recognition interaction. Affinity ligands, based on the peptide structure, can be peptides, peptide-mimetic derivatives (<30 monomers) and microproteins (e.g. 25-200 monomers). Microprotein ligands are selected from biological libraries constructed of variegated protein domains, e.g. minibody, Kunitz, tendamist, cellulose-binding domain, scFv, Cytb562, zinc-finger, SpA-analogue (Z-domain). © 2005 Elsevier B.V. All rights reserved.	en
heal.journalName	Journal of Chromatography A	en
dc.identifier.issue	1-2	en
dc.identifier.volume	1101	en
dc.identifier.doi	10.1016/j.chroma.2005.09.073	en
dc.identifier.spage	1	en
dc.identifier.epage	24	en