CAMPERI Silvia Andrea
capítulos de libros
Single step recombinant human follicle stimulating hormone purification by peptide affinity chromatography
S. L. GIUDICESSI; M. C. MARTÍNEZ CERON; N. URTASUN; L. MAURO; G. FORNO; O. CASCONE; CAMPERI, S.A.
Proceedings of the 35th European Peptide Symposium
Año: 2019; p. 127 - 129
Human Follicle Stimulating Hormone(hFSH) is clinically used for ovulation in women and spermatogenesisinductionin men, in assisted reproduction technologies (1). As FSH-based biopharmaceuticals areparenterally administered, their purity must be high. Current methods for hFSH purification include severalchromatographic steps to reach the required purity. However, these involve a decrease in the hFSH total yieldand rises the cost of the process. Affinity chromatography (AC) consists in the specific adsorption of targetbiomolecules onto ligands immobilized on chromatographic supports. Short peptides have been described asuseful ligands for AC because of their low cost, simple chemical synthesis and high stability compared toprotein-based ligands (2). The aim of this work was to design an affinity chromatography matrix with animmobilized synthetic peptide for rhFSH purification.