ArticleFrontiers in immunology2014
Interactions of IgG1 CH2 and CH3 Domains with FcRn.
Article in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 44 citations in OpenAlex.
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- Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.Nature communications · 2024Article
- Half-life extension of single-domain antibody-drug conjugates by albumin binding moiety enhances antitumor efficacy.MedComm · 2024Article
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- Structure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines.Antibodies (Basel, Switzerland) · 2023Review
- The Generation of Dual-Targeting Fusion Protein PD-L1/CD47 for the Inhibition of Triple-Negative Breast Cancer.Biomedicines · 2022Article
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- The Role of Bispecific Antibodies in Non-Hodgkin's Lymphoma: From Structure to Prospective Clinical Use.Antibodies (Basel, Switzerland) · 2022Review
- Rapid Production of Bispecific Antibodies from Off-the-Shelf IgGs with High Yield and Purity.Bioconjugate chemistry · 2022Article
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- Hairpin Oligonucleotide Can Functionalize Gold Nanorods forACS omega · 2020Article
- Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis.RSC advances · 2020Article
- An explorative study towards the chemical synthesis of the immunoglobulin G1 Fc CH3 domain.Journal of peptide science : an official publication of the European Peptide Society · 2018Article
- Single-Domain Antibodies As Therapeutics against Human Viral Diseases.Frontiers in immunology · 2017Review
- Engineered Soluble Monomeric IgG1 Fc with Significantly Decreased Non-Specific Binding.Frontiers in immunology · 2017Article
- Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds.Frontiers in immunology · 2017Review
- Bispecific Antibodies as a Development Platform for New Concepts and Treatment Strategies.International journal of molecular sciences · 2016Review
- Development of human neutralizing monoclonal antibodies for prevention and therapy of MERS-CoV infections.Microbes and infection · 2015Review
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Antibody fragments are emerging as promising biopharmaceuticals because of their relatively small-size and other unique properties. However, when compared to full-size antibodies, most of the current antibody fragments of VH or VL display greatly reduced half-lives. A promising approach to overcome this problem is through the development of novel antibody fragments based on IgG Fc region, which contributes to the long half-life of IgG through its unique pH-dependent association with the neonatal Fc receptor (FcRn). The IgG Fc region comprises two CH2 and two CH3 domains. In this report, we present a comparative study of the FcRn binding capability of the CH2 and CH3 domains. The stability and aggregation resistance of these domains were also investigated and compared. We found that monomeric CH2 and CH3 domains exhibited the pH-dependent FcRn binding while the dimeric forms of CH2 and CH3 domains did not. Although all of these domains had high serum stability, they had aggregation tendencies as measured by dynamic light scattering. By providing a better understanding of the structure-activity relationship of the Fc fragment, these results guide further approaches to generate novel Fc-based small-size antibody fragments that possess pH-dependent FcRn binding capability, desired in vivo half-lives, and other favorable biophysical properties for their druggability.
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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.