ArticleThe Journal of biological chemistry2009
Engineered human antibody constant domains with increased stability.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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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.
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Who cites it
46 citing papers in PubMed, 92 citations in OpenAlex.
- Highly potent C-type nanoantibodies neutralize Nipah and Hendra viruses by cavity filling on fusion glycoprotein.Nature communications · 2026Article
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- Enhancing thermal stability in the CHProtein science : a publication of the Protein Society · 2023Article
- Arginine cluster introduction on framework region in anti-lysozyme antibody improved association rate constant by changing conformational diversity of CDR loops.Protein science : a publication of the Protein Society · 2023Article
- Antibody stabilization for thermally accelerated deep immunostaining.Nature methods · 2022Article
- The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021Article
- An off-the-Shelf Approach for the Production of Fc Fusion Proteins by ProteinInternational journal of molecular sciences · 2020Article
- Improvement in affinity and thermostability of a fully human antibody against interleukin-17A by yeast-display technology and CDR grafting.Acta pharmaceutica Sinica. B · 2019Article
- Evaluation of a noncanonical Cys40-Cys55 disulfide linkage for stabilization of single-domain antibodies.Protein science : a publication of the Protein Society · 2019Article
- Comprehensive elucidation of the structural and functional roles of engineered disulfide bonds in antibody Fc fragment.The Journal of biological chemistry · 2018Article
- Effects of localized interactions and surface properties on stability of protein-based therapeutics.The Journal of pharmacy and pharmacology · 2018Review
- Article
- Engineered antibody CH2 domains binding to nucleolin: Isolation, characterization and improvement of aggregation.Biochemical and biophysical research communications · 2017Article
- Engineering an IgG Scaffold Lacking Effector Function with Optimized Developability.The Journal of biological chemistry · 2017Article
- Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.Frontiers in immunology · 2017Review
- Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds.Frontiers in immunology · 2017Review
- Antibody Aggregation: Insights from Sequence and Structure.Antibodies (Basel, Switzerland) · 2016Review
- Comparison of Tobacco Host Cell Protein Removal Methods by Blanching Intact Plants or by Heat Treatment of Extracts.Journal of visualized experiments : JoVE · 2016Article
- Engineered IgG1-Fc--one fragment to bind them all.Immunological reviews · 2016Review
- Construction of polyomavirus-derived pseudotype virus-like particles displaying a functionally active neutralizing antibody against hepatitis B virus surface antigen.BMC biotechnology · 2015Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The immunoglobulin (Ig) constant CH2 domain is critical for antibody effector functions. Isolated CH2 domains are promising as scaffolds for construction of libraries containing diverse binders that could also confer some effector functions. However, previous work has shown that an isolated murine CH2 domain is relatively unstable to thermally induced unfolding. To explore unfolding mechanisms of isolated human CH2 and increase its stability gamma1 CH2 was cloned and a panel of cysteine mutants was constructed. Human gamma1 CH2 unfolded at a higher temperature (T(m) = 54.1 degrees C, as measured by circular dichroism) than that previously reported for a mouse CH2 (41 degrees C). One mutant (m01) was remarkably stable (T(m) = 73.8 degrees C). Similar results were obtained by differential scanning calorimetry. This mutant was also significantly more stable than the wild-type CH2 against urea induced unfolding (50% unfolding at urea concentration of 6.8 m versus 4.2 m). The m01 was highly soluble and monomeric. The existence of the second disulfide bond in m01 and its correct position were demonstrated by mass spectrometry and nuclear magnetic resonance spectroscopy, respectively. The loops were on average more flexible than the framework in both CH2 and m01, and the overall secondary structure was not affected by the additional disulfide bond. These data suggest that a human CH2 domain is relatively stable to unfolding at physiological temperature, and that both CH2 and the highly stable mutant m01 are promising new scaffolds for the development of therapeutics against human diseases.
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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.