Preparation of monoPEGylated human interferon beta-1a: Optimization of the conditions for N-terminal PEGylation

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 c...

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Bibliographic Details
Published in:Applied biochemistry and microbiology 2015-12, Vol.51 (7), p.774-785
Main Authors: Korzhavin, D. V, Chernovskaya, T. V, Efanov, Yu. G, Rudenko, E. G, Ivanov, R. A, Pshenichnikova, A. B, Shvets, V. I
Format: Article
Language:English
Subjects:
antiviral properties
Biochemistry
Biomedical and Life Sciences
chemical bonding
chromatography
humans
Interferon
interferons
Life Sciences
Medical Microbiology
medicine
methionine
Microbiology
molecular weight
Optimization techniques
Polyethylene glycol
sclerosis
Technology of Biopreparations
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Summary: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.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683815070030