Purification of dirucotide, a synthetic 17-aminoacid peptide, by ion exchange centrifugal partition chromatography

  • J Chromatogr A. 2017 Sep 1;1513:78-83. doi: 10.1016/j.chroma.2017.07.003.
Leslie Boudesocque  1 ,  Luciano Forni  2 ,  Agathe Martinez  3 ,  Jean-Marc Nuzillard  3 ,  Matthieu Giraud  2 ,  Jean-Hugues Renault  4
Affiliations
  • 1. Institut de Chimie Moléculaire de Reims UMR CNRS 7312, SFR Cap'Santé, Université de Reims Champagne-Ardenne, Reims, France; UMR INRA 1282 Infectiologie Santé Publique, Université de Tours François Rabelais, UFR Sciences Pharmaceutiques Philippe Maupas, Tours, France.
  • 2. Lonza Ltd, Valais Work CH-3930 Visp, Switzerland.
  • 3. Institut de Chimie Moléculaire de Reims UMR CNRS 7312, SFR Cap'Santé, Université de Reims Champagne-Ardenne, Reims, France.
  • 4. Institut de Chimie Moléculaire de Reims UMR CNRS 7312, SFR Cap'Santé, Université de Reims Champagne-Ardenne, Reims, France. Electronic address: [email protected].
PMID: 28739271 DOI: 10.1016/j.chroma.2017.07.003
Abstract

Dirucotide is a synthetic drug candidate for the treatment of multiple sclerosis. This 17-aminoacid peptide was successfully purified by ion exchange centrifugal partition chromatography. The optimized conditions involved the biphasic methyl tert-butyl ether/acetonitrile/n-butanol/water (2:1:2:5, v/v) solvent system in the descending mode, the di(2-ethylhexyl)phosphoric acid cation-exchanger with an exchanger (di(2-ethylhexyl)phosphoric acid)/dirucotide mole ratio of 100 and CA2+ ions in aqueous solution as displacer. Critical impurities were efficiently eliminated and dirucotide was recovered in high yield and purity (69% and 98%, respectively) and with a productivity of 2.29g per liter of stationary phase per hour.

Keywords
Bioactive peptide; Centrifugal partition chromatography; Dirucotide; Ion exchange; Multiple sclerosis.
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