ArticleFrontiers in immunology2017
Engineered Soluble Monomeric IgG1 Fc with Significantly Decreased Non-Specific Binding.
Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Direct Selection of Functional De Novo Macrocycles for Activation of On-Cellulo Insulin Receptor.Angewandte Chemie (International ed. in English) · 2026Article
- Topical delivery of a human single-domain antibody targeting IL-33 to inhibit mucosal inflammation.Cellular & molecular immunology · 2025Article
- Enhancing vaccine half-life as a novel strategy for improving immune response durability of subunit vaccines.PLoS pathogens · 2025Article
- Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.Nature communications · 2024Article
- Immobilized enzyme cascade for targeted glycosylation.Nature chemical biology · 2024Article
- Research Advances in Fusion Protein-Based Drugs for Diabetes Treatment.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024Review
- Anti-VEGFR2 F(ab')Nature communications · 2023Article
- Engineering an Enhanced EGFR Engager: Humanization of Cetuximab for Improved Developability.Antibodies (Basel, Switzerland) · 2022Article
- Reteplase Fc-fusions produced in N. benthamiana are able to dissolve blood clots ex vivo.PloS one · 2021Article
- The Instability of Dimeric Fc-Fusions Expressed in Plants Can Be Solved by Monomeric Fc Technology.Frontiers in plant science · 2021Article
- Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis.RSC advances · 2020Article
- Boosting therapeutic potency of antibodies by taming Fc domain functions.Experimental & molecular medicine · 2019Review
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Due to the long serum half-life provided by the neonatal Fc receptor (FcRn) recycling, the IgG1 Fc has been pursued as the fusion partner to develop therapeutic Fc-fusion proteins, or as the antibody-derived scaffold that could be engineered with antigen-binding capabilities. In previous studies, we engineered the monomeric Fc by mutating critical residues located on the IgG1 Fc dimerization interface. Comparing with the wild-type dimeric Fc, monomeric Fc might possess substantial advantages conferred by its smaller size, but also suffers the disadvantage of non-specific binding to some unrelated antigens, raising considerable concerns over its potential clinical development. Here, we describe a phage display-based strategy to examine the effects of multiple mutations of IgG1 monomeric Fc and, simultaneously, to identify new Fc monomers with desired properties. Consequently, we identified a novel monomeric Fc that displayed significantly decreased non-specificity. In addition, it exhibited higher thermal stability and comparable pH-dependent FcRn binding to the previous reported monomeric Fc. These results provide baseline to understand the mechanism underlying the generation of soluble IgG1 Fc monomers and warrant the further clinical development of monomeric Fc-based fusion proteins as well as antigen binders.
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