IngentaConnect Stability of Ala 125 recombinant human interleukin-2 in solution

Authors: Nuria Reyes¹; Llamil Ruiz¹; Kethia Aroche¹; Haydee Gerónimo¹; Olga Brito¹; Eugenio Hardy¹

Source: Journal of Pharmacy and Pharmacology, Volume 57, Number 1, January 2005 , pp. 31-37(7)

Abstract:

Herein, we describe the preformulation study of Ala 125- recombinant human interleukin-2 (rhIL-2A¹²⁵) in solution. This modified form of the natural human IL-2 is obtained by the replacement of cysteine with alanine at position 125. The compatibility of this rhIL-2A¹²⁵ with type I borosilicate glass vials showed no significant adsorption at liquid–vial interface. The effect of single excipients on the stability of this lymphokine was evaluated through RP-HPLC, SDS-PAGE and biological activity assay. Polysorbate 80 at high concentrations decreased the stability of rhIL-2A¹²⁵ in solution. On the other hand, the use of antioxidants (methionine and EDTA Na₂) diminished the oxidation rate of the active ingredient. Additionally, a group of amino acids (glutamine, alanine, glycine and histidine) stabilized rhIL-2A¹²⁵ in different grades, and glycine at 5 mg mL^-1 allowed for the best stability behaviour. Taken together, these preformulation results can be used to design an adequate liquid vehicle for rhIL-2A¹²⁵ to be manufactured for human use.

Document Type: Research article

DOI: 10.1211/0022357055182

Affiliations: 1: Center for Genetic Engineering and Biotechnology, P. O. Box 6162, Havana, Cuba

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$38.49 plus tax Refund Policy