ArticleProtein science : a publication of the Protein Society2008
Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed.
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- Characterization of a Monoclonal Antibody by Native and Denaturing Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Structural Characterization of Disulfide-Linked p53-Derived Peptide Dimers.Research square · 2024Article
- Missense3D-PPI: A Web Resource to Predict the Impact of Missense Variants at Protein Interfaces Using 3D Structural Data.Journal of molecular biology · 2023Article
- Stability Determination of Intact Humanin-G with Characterizations of Oxidation and Dimerization Patterns.Biomolecules · 2023Article
- Construction of scFv Antibodies against the Outer Loops of the MicrosporidiumInternational journal of molecular sciences · 2022Article
- Point mutations in SARS-CoV-2 variants induce long-range dynamical perturbations in neutralizing antibodies.Chemical science · 2022Article
- Emulation of the structure of the Saposin protein fold by a lung surfactant peptide construct of surfactant Protein B.PloS one · 2022Article
- Cysteine in cell culture media induces acidic IgG1 species by disrupting the disulfide bond network.Biotechnology and bioengineering · 2021Article
- Antibody conjugation and formulation.Antibody therapeutics · 2019Review
- Comprehensive elucidation of the structural and functional roles of engineered disulfide bonds in antibody Fc fragment.The Journal of biological chemistry · 2018Article
- Complementary middle-down and intact monoclonal antibody proteoform characterization by capillary zone electrophoresis - mass spectrometry.Electrophoresis · 2018Article
- An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity.Cell stress & chaperones · 2018Article
- Antibody-Drug Conjugates for Cancer Therapy: Chemistry to Clinical Implications.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Assigning Peptide Disulfide Linkage Pattern Among Regio-Isomers via Methoxy Addition to Disulfide and Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
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10 authors.
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Abstract
Recombinant human monoclonal antibodies have become important protein-based therapeutics for the treatment of various diseases. The antibody structure is complex, consisting of beta-sheet rich domains stabilized by multiple disulfide bridges. The dimerization of the C(H)3 domain in the constant region of the heavy chain plays a pivotal role in the assembly of an antibody. This domain contains a single buried, highly conserved disulfide bond. This disulfide bond was not required for dimerization, since a recombinant human C(H)3 domain, even in the reduced state, existed as a dimer. Spectroscopic analyses showed that the secondary and tertiary structures of reduced and oxidized C(H)3 dimer were similar, but differences were observed. The reduced C(H)3 dimer was less stable than the oxidized form to denaturation by guanidinium chloride (GdmCl), pH, or heat. Equilibrium sedimentation revealed that the reduced dimer dissociated at lower GdmCl concentration than the oxidized form. This implies that the disulfide bond shifts the monomer-dimer equilibrium. Interestingly, the dimer-monomer dissociation transition occurred at lower GdmCl concentration than the unfolding transition. Thus, disulfide bond formation in the human C(H)3 domain is important for stability and dimerization. Here we show the importance of the role played by the disulfide bond and how it affects the stability and monomer-dimer equilibrium of the human C(H)3 domain. Hence, these results may have implications for the stability of the intact antibody.
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