Journal
PLOS ONE
Volume 9, Issue 5, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0096967
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Funding
- Basic Science Research Program through the National Research Foundation (NRF) [NRF-2012R1A1A1043288]
- Korea Drug Development Fund of Korea - Ministry of Education, Science and Technology [20100030032]
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The purpose of this study was to develop a biobetter version of recombinant human interferon-beta 1a (rhIFN-beta 1a) to improve its biophysical properties, such as aggregation, production and stability, and pharmacokinetic properties without jeopardizing its activity. To achieve this, we introduced additional glycosylation into rhIFN-beta 1a via site-directed mutagenesis. Glycoengineering of rhIFN-beta 1a resulted in a new molecular entity, termed R27T, which was defined as a rhIFN-beta mutein with two N-glycosylation sites at 80th (original site) and at an additional 25th amino acid due to a mutation of Thr for Arg at position 27th of rhIFN-beta 1a. Glycoengineering had no effect on rhIFN-beta ligand-receptor binding, as no loss of specific activity was observed. R27T showed improved stability and had a reduced propensity for aggregation and an increased half-life. Therefore, hyperglycosylated rhIFN-beta could be a biobetter version of rhIFN-beta 1a with a potential for use as a drug against multiple sclerosis.
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