ArticleInternational journal of molecular sciences2014
Molecular dynamics simulation of the crystallizable fragment of IgG1-insights for the design of Fcabs.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Effects of glycans and hinge on dynamics in the IgG1 Fc.Journal of biomolecular structure & dynamics · 2024Article
- Glycosylation of Plant-Produced Immunoglobulins.Experientia supplementum (2012) · 2021Article
- Modeling and Molecular Dynamic Simulation of F(ab')Bioinformatics and biology insights · 2021Article
- Designing antibody against highly conserved region of dengue envelope protein by in silico screening of scFv mutant library.PloS one · 2019Article
- Thinking outside the Laboratory: Analyses of Antibody Structure and Dynamics within Different Solvent Environments in Molecular Dynamics (MD) Simulations.Antibodies (Basel, Switzerland) · 2018Article
- Engineered IgG1-Fc--one fragment to bind them all.Immunological reviews · 2016Review
- Article
- Creating stable stem regions for loop elongation in Fcabs - insights from combining yeast surface display, in silico loop reconstruction and molecular dynamics simulations.Biochimica et biophysica acta · 2014Article
- Construction of pH-sensitive Her2-binding IgG1-Fc by directed evolution.Biotechnology journal · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
An interesting format in the development of therapeutic monoclonal antibodies uses the crystallizable fragment of IgG1 as starting scaffold. Engineering of its structural loops allows generation of an antigen binding site. However, this might impair the molecule's conformational stability, which can be overcome by introducing stabilizing point mutations in the CH3 domains. These point mutations often affect the stability and unfolding behavior of both the CH2 and CH3 domains. In order to understand this cross-talk, molecular dynamics simulations of the domains of the Fc fragment of human IgG1 are reported. The structure of human IgG1-Fc obtained from X-ray crystallography is used as a starting point for simulations of the wild-type protein at two different pH values. The stabilizing effect of a single point mutation in the CH3 domain as well as the impact of the hinge region and the glycan tree structure connected to the CH2 domains is investigated. Regions of high local flexibility were identified as potential sites for engineering antigen binding sites. Obtained data are discussed with respect to the available X-ray structure of IgG1-Fc, directed evolution approaches that screen for stability and use of the scaffold IgG1-Fc in the design of antigen binding Fc proteins.
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Registered trials
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