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- Publisher
- Springer Journals
- Copyright
- Copyright © 2015 by Pleiades Publishing, Inc.
- Subject
- Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
- ISSN
- 0003-6838
- eISSN
- 1608-3024
- DOI
- 10.1134/S0003683815070030
- Publisher site
- See Article on Publisher Site
Abstract
The recombinant human interferon (IFN) beta-1a was modified with polyethylene glycol (PEG). The reaction was performed with the use of activated linear butyraldehyde PEG derivative with a molecular weight of 30 kDa. As a result of the multifactorial experiment, the correlation between the reaction conditions and the yield of the monoPEGylated protein was demonstrated and the optimal PEGylation conditions were established. We developed a one-step chromatographic purification scheme that makes it possible to obtain monoPEG-IFN beta-1a conjugate a purity above 98%. Mass-spectrometric studies showed that the purified conjugate is the PEGylated IFN beta-1a, in which the N-terminal methionine is bound with a PEG molecule. The molecular weight of the conjugate is 54130 Da. The obtained PEG-IFN beta-1a has a specific antiviral activity; it can be considered as a promising candidate in the design of prolonged-release medicine for the treatment of multiple sclerosis.
Journal
Applied Biochemistry and Microbiology – Springer Journals
Published: Oct 23, 2015