ArticleJournal of pharmaceutical sciences2014
Physical stability comparisons of IgG1-Fc variants: effects of N-glycosylation site occupancy and Asp/Gln residues at site Asn 297.
Article in Journal of pharmaceutical sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.The Biochemical journal · 2026Article
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- Evaluation of Phage Display Biopanning Strategies for the Selection of Anti-Cell Surface Receptor Antibodies.International journal of molecular sciences · 2022Article
- Process- and Product-Related Foulants in Virus Filtration.Bioengineering (Basel, Switzerland) · 2022Review
- Fc Galactosylation Promotes Hexamerization of Human IgG1, Leading to Enhanced Classical Complement Activation.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Solution structure of deglycosylated human IgG1 shows the role of CBiophysical journal · 2021Article
- Homogeneous production and characterization of recombinant N-GlcNAc-protein in Pichia pastoris.Microbial cell factories · 2020Article
- Effects of localized interactions and surface properties on stability of protein-based therapeutics.The Journal of pharmacy and pharmacology · 2018Review
- Article
- Synthesis of a Bifunctional Peptide Inhibitor-IgG1 Fc Fusion That Suppresses Experimental Autoimmune Encephalomyelitis.Bioconjugate chemistry · 2017Article
- A Multidimensional Analytical Comparison of Remicade and the Biosimilar Remsima.Analytical chemistry · 2017Article
- Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.Frontiers in immunology · 2017Review
- Assessment of Hepatocellular Carcinoma Metastasis Glycobiomarkers Using Advanced Quantitative N-glycoproteome Analysis.Frontiers in physiology · 2017Article
- Comparative Evaluation of the Chemical Stability of 4 Well-Defined Immunoglobulin G1-Fc Glycoforms.Journal of pharmaceutical sciences · 2016Article
- Production, Characterization, and Biological Evaluation of Well-Defined IgG1 Fc Glycoforms as a Model System for Biosimilarity Analysis.Journal of pharmaceutical sciences · 2016Article
- Review
- Effects of different interchain linkers on biological activity of an anti-prostate cancer single-chain bispecific antibody.Theoretical biology & medical modelling · 2015Article
- Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation.Protein science : a publication of the Protein Society · 2015Article
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The structural integrity and conformational stability of various IgG1-Fc proteins produced from the yeast Pichia pastoris with different glycosylation site occupancy (di-, mono-, and nonglycosylated) were determined. In addition, the physical stability profiles of three different forms of nonglycosylated Fc molecules (varying amino-acid residues at site 297 in the CH 2 domain due to the point mutations and enzymatic digestion of the Fc glycoforms) were also examined. The physical stability of these IgG1-Fc glycoproteins was examined as a function of pH and temperature by high-throughput biophysical analysis using multiple techniques combined with data visualization tools (three index empirical phase diagrams and radar charts). Across the pH range of 4.0-6.0, the di- and monoglycosylated forms of the IgG1-Fc showed the highest and lowest levels of physical stability, respectively, with the nonglycosylated forms showing intermediate stability depending on solution pH. In the aglycosylated Fc proteins, the introduction of Asp (D) residues at site 297 (QQ vs. DN vs. DD forms) resulted in more subtle changes in structural integrity and physical stability depending on solution pH. The utility of evaluating the conformational stability profile differences between the various IgG1-Fc glycoproteins is discussed in the context of analytical comparability studies.
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