Abstract
A modification of recombinant human IFN beta- 1a by polyethylene glycol at a-amino group of N-terminal methionine has been performed. The PEGylation was conducted using activated butyraldehyde PEG derivative with molecular mass of 30000 Da. As a result of the multifactorial experiment, the dependence of monoPEGylated protein yield on the reaction conditions was demonstrated, and optimal PEGylation conditions were established. We developed a one-step chromatographic purification scheme allowing to obtain the monoPEG-IFN beta-1a conjugate with the above 98% purity . Mass-spectrometric studies showed that the molecular mass of the conjugate is 54130 Da, wherein the N-terminal methionine is associated with one PEG molecule. The obtained PEG-IFN beta-1a has specific antiviral activity, and it can be considered as a perspective candidate to the design of long-acting medicine for the prolonged treatment of multiple sclerosis.
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