ArticleMolecules (Basel, Switzerland)2024
LC-MS/MS-Based Site-Specific N-Glycosylation Analysis of VEGFR-IgG Fusion Protein for Sialylation Assessment Across IEF Fractions.
Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
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.
Funding
Abstract
The glycosylation profile of therapeutic proteins significantly influences their efficacy, stability, and immunogenicity. Sialylation is crucial for the biological activity and pharmacokinetics of fusion proteins used in treating angiogenic disorders, making sialic acid levels a critical quality attribute in the development and production of biologics. In this study, we employed a mass spectrometry-based approach to assess sialylation levels through site-specific N-glycosylation analysis. To validate the method's effectiveness, IEF fractions (acidic, main, and basic) obtained from the production media of the VEGFR-IgG fusion protein and anticipated to exhibit varying sialylation levels were analyzed. Our analytical method successfully evaluated the sialylation levels of each domain-IgG, VEGFR-1, and VEGFR-2-within the Fc-fusion protein. The results confirm that the overall sialylation level of the Fc-fusion protein correlated with the levels observed across the IEF fractions. This finding highlights the value of LC-MS/MS-based sialylation monitoring as a crucial tool for biosimilar development and quality control, particularly in optimizing target protein production. Additionally, glycopeptide-based LC-MS analysis enables site-specific sialylation evaluation, ensuring consistent profiles for robust quality assurance.
Indexed as
Identifiers
What OpenQuestion holds
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.