Isolation of a peptide ligand for affinity purification of factor VIII using phage display

Journal of Chromatography. a
B D KelleyArthur C Ley

Abstract

Polypeptides for use in affinity chromatography of factor VIII were identified using phage display technology. Phage libraries were designed to express polypeptide fusions containing five to seven residues flanked by two cysteines that form a disulfide bond. Individual bacteriophage were selected for the ability of these polypeptides to bind factor VIII, and then release the protein under mild elution conditions. Strong consensus sequences were observed that appear to be necessary for this reversible interaction. Chemically synthesized ligands identified by this screening were immobilized onto a chromatographic support and used for affinity purification of factor VIII from a complex feedstream. A chromatographic step was developed that provided a 10000-fold reduction in host cell proteins and DNA, while providing exceptional product recovery.

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Citations

Feb 2, 2010·The Journal of Biological Chemistry·Chen QianJing Zhang
Mar 25, 2014·Biotechnology Letters·Dongli Guan, Zhilei Chen
Nov 13, 2007·Biologicals : Journal of the International Association of Biological Standardization·Brian D KelleySteven Vicik
Apr 24, 2010·Haemophilia : the Official Journal of the World Federation of Hemophilia·J WindygaS Arkin
Jan 1, 2010·Haemophilia : the Official Journal of the World Federation of Hemophilia·B KelleyJ Booth
Mar 3, 2006·Analytical Biochemistry·Dina WassafDaniel J Sexton
Aug 30, 2016·Biotechnology and Bioengineering·Ana M G C Dias, Ana C A Roque
Jun 22, 2005·Expert Review of Proteomics·Sun W TamDouglas Hinerfeld
Feb 15, 2007·Journal of Chromatography. a·Fu-Feng LiuYan Sun
Apr 26, 2018·Biotechnology Progress·John P TrasattiPankaj Karande
May 7, 2019·Pharmaceutics·Esen SokulluMarc A Gauthier
Jul 1, 2014·Langmuir : the ACS Journal of Surfaces and Colloids·Yanying LiYan Sun

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