PASylation technology improves recombinant interferon-ß1b solubility, stability, and biological activity.
Appl Microbiol Biotechnol
; 101(5): 1975-1987, 2017 Mar.
Article
en En
| MEDLINE
| ID: mdl-27833991
ABSTRACT
Recombinant interferon-ß1b (IFN-ß1b) is an effective remedy against multiple sclerosis and other diseases. However, use of small polypeptide (molecular weight is around 18.5 kDa) is limited due to poor solubility, stability, and short half-life in systemic circulation. To solve this problem, we constructed two variants of PASylated IFN-ß1b, with PAS sequence at C- or N-terminus of IFN-ß1b. The PAS-modified proteins demonstrated 4-fold increase in hydrodynamic volume of the molecule combined with 2-fold increase of in vitro biological activity, as well as advanced stability and solubility of the protein in solution as opposed to unmodified IFN-ß1b. Our results demonstrate that PASylation has a positive impact on stability, solubility, and functional activity of IFN-ß1b and potentially might improve pharmacokinetic properties of the molecule as a therapeutic agent.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Recombinantes
/
Procesamiento Proteico-Postraduccional
/
Interferon beta-1b
/
Factores Inmunológicos
Límite:
Humans
Idioma:
En
Revista:
Appl Microbiol Biotechnol
Año:
2017
Tipo del documento:
Article
País de afiliación:
Rusia