| Literature DB >> 27833991 |
Elizaveta A Zvonova1, Alexander V Ershov2, Olga A Ershova2, Marina A Sudomoina3, Maksim B Degterev3, Grigoriy N Poroshin3, Artem V Eremeev4, Andrey P Karpov4, Alexander Yu Vishnevsky3, Irina V Goldenkova-Pavlova5, Andrei V Petrov6, Sergey V Ruchko4, Alexander M Shuster3.
Abstract
Recombinant interferon-β1b (IFN-β1b) 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-β1b, with PAS sequence at C- or N-terminus of IFN-β1b. 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-β1b. Our results demonstrate that PASylation has a positive impact on stability, solubility, and functional activity of IFN-β1b and potentially might improve pharmacokinetic properties of the molecule as a therapeutic agent.Entities:
Keywords: Biological activity; Expression; Interferon-β1b; PASylation; Solubility; Stability
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Year: 2016 PMID： 27833991 DOI： 10.1007/s00253-016-7944-3
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN： 0175-7598 Impact factor: 4.813