ArticlePharmaceutical research2011
O-linked glycosylation leads to decreased thermal stability of interferon alpha 2b as measured by two orthogonal techniques.
Article in Pharmaceutical research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Synthesis and Optimization of PEG-PLGA Immunotherapeutic Nanoparticles for the Controlled Release of IFNα.AAPS PharmSciTech · 2026Article
- Highly selective split intein method for efficient separation and purification of recombinant therapeutic proteins from mammalian cell culture fluid.Journal of chromatography. A · 2024Article
- Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems.International journal of molecular sciences · 2024Article
- Effects of localized interactions and surface properties on stability of protein-based therapeutics.The Journal of pharmacy and pharmacology · 2018Review
- Article
- A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon α2a around the glycosylation site.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThermal stability is considered an indication of protein fold and conformational stability. We investigate the influence of glycosylation on the thermal stability of interferon alpha 2b (IFN α-2b).
methodsFar ultraviolet light circular dichroism spectroscopy (UV CD) and differential scanning calorimetry (DSC) were used to assess the thermal stability of the European Directorate for the Quality of Medicines IFN α-2b reference standards as well as an O-linked glycosylated IFN α-2b produced in human embryonic kidney cells.
resultsAssessment of thermal stability of IFN α-2b and glycosylated IFN α-2b by DSC revealed that non-glycosylated interferon (Tm=65.7 +/- 0.2°C, n=3) was more thermally stable than the glycosylated variant (Tm=63.8 C +/- 0.4°C, n=3). These observations were confirmed with far UV CD (Tm IFN α-2b=65.3 +/- 0.4°C, Tm glycosylated IFN α-2b=63.6 +/- 0.2°C, n=3). Enzymatic deglycosylation of IFN α-2b resulted in improved thermally stability when assessed with far UV CD and DSC.
conclusionWe demonstrate that O-linked glycosylation decreases the thermal stability of IFN α-2b compared to a non-glycosylated variant of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.