ArticleJournal of pharmaceutical sciences2016
Production, Characterization, and Biological Evaluation of Well-Defined IgG1 Fc Glycoforms as a Model System for Biosimilarity Analysis.
Article in Journal of pharmaceutical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Fully human recombinant antibodies against EphA2 from a multi-tumor patient immune library suitable for tumor-targeted therapy.Bioengineered · 2021Article
- Activity of CcpA-Regulated GH18 Family Glycosyl Hydrolases That Contributes to Nutrient Acquisition and Fitness in Enterococcus faecalis.Infection and immunity · 2021Article
- Comparative studies on the substrate specificity and defucosylation activity of three α-l-fucosidases using synthetic fucosylated glycopeptides and glycoproteins as substrates.Bioorganic & medicinal chemistry · 2021Article
- A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function.Glycobiology · 2020Review
- The Impact of Immunoglobulin G1 Fc Sialylation on Backbone Amide H/D Exchange.Antibodies (Basel, Switzerland) · 2019Article
- Article
- Impact of Glycosylation on the Local Backbone Flexibility of Well-Defined IgG1-Fc Glycoforms Using Hydrogen Exchange-Mass Spectrometry.Journal of pharmaceutical sciences · 2018Article
- In Silico Methods in Antibody Design.Antibodies (Basel, Switzerland) · 2018Review
- Structural characterization of the Man5 glycoform of human IgG3 Fc.Molecular immunology · 2017Article
- A library of chemically defined human N-glycans synthesized from microbial oligosaccharide precursors.Scientific reports · 2017Article
- Comparative Characterization of Crofelemer Samples Using Data Mining and Machine Learning Approaches With Analytical Stability Data Sets.Journal of pharmaceutical sciences · 2017Article
- The Botanical Drug Substance Crofelemer as a Model System for Comparative Characterization of Complex Mixture Drugs.Journal of pharmaceutical sciences · 2017Article
- Effects of N-Glycan Composition on Structure and Dynamics of IgG1 Fc and Their Implications for Antibody Engineering.Scientific reports · 2017Article
- 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
- Comparative Evaluation of the Chemical Stability of 4 Well-Defined Immunoglobulin G1-Fc Glycoforms.Journal of pharmaceutical sciences · 2016Article
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Authors and funding
9 authors.
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Abstract
Four different well-defined IgG1 Fc glycoforms are proposed as a model system to examine important biological and physicochemical features for protein drug biosimilar analyses. The IgG1 Fc glycoforms were produced by yeast expression combined with in vitro enzymatic synthesis as a series of sequentially truncated high-mannose IgG1 Fc glycoforms with an anticipated range of biological activity and structural stability. Initial characterization with mass spectrometry, SDS-PAGE, size exclusion HPLC, and capillary isoelectric focusing confirmed that the glycoproteins are overall highly similar with the only major difference being glycosylation state. Binding to the activating Fc receptor, FcγRIIIa was used to evaluate the potential biological activity of the IgG1 Fc glycoproteins. Two complementary methods using biolayer interferometry, 1 with protein G-immobilized IgG1 Fc and the other with streptavidin-immobilized FcγRIIIa, were developed to assess FcγRIIIa affinity in kinetic binding studies. The high-mannose IgG1 Fc and Man5-IgG1 Fc glycoforms were highly similar to one another with high affinity for FcγRIIIa, whereas GlcNAc-Fc had weak affinity, and the nonglycosylated N297Q-Fc had no measurable affinity for FcγRIIIa. These 4 IgG1 Fc glycoforms were also evaluated in terms of physical and chemical stability profiles and then used as a model system to mathematically assess overall biosimilarity, as described in a series of companion articles.
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Registered trials
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