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

Date publication

juillet 2017

Journal

Journal of chromatography. A

Auteurs

Membres identifiés du Cancéropôle Est :
Dr NUZILLARD Jean-Marc

Tous les auteurs :
Boudesocque L, Forni L, Martinez A, Nuzillard JM, Giraud M, Renault JH

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/28739271

Résumé

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 Ca(2+) 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.

Mots clés

Bioactive peptide, Centrifugal partition chromatography, Dirucotide, Ion exchange, Multiple sclerosis

Référence

J Chromatogr A. 2017 Jul;: