ArticleRSC advances2020
Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Application of Computational Techniques in Antibody Fc-Fused Molecule Design for Therapeutics.Molecular biotechnology · 2024Review
- FcRn inhibitors: a novel option for the treatment of myasthenia gravis.Neural regeneration research · 2023Review
- Anti-TNF Alpha Antibody Humira with pH-dependent Binding Characteristics: A constant-pH Molecular Dynamics, Gaussian Accelerated Molecular Dynamics, and In Vitro Study.Biomolecules · 2021Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding of IgG Fc with FcRn enables the long circulating half-life of IgG, where the Fc-FcRn complex interacts in a pH-dependent manner. This complex shows stronger interaction at pH ≤ 6.5 and weaker interaction at pH ≥ 7.4. The Fc-FcRn binding mechanism that promotes the long circulating half-life of IgG has prompted several IgG Fc-related mutational studies to focus on the pH-dependent Fc-FcRn complex interactions in order to improve the pharmacokinetic properties of Fc. Hence, in this study, we applied the
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Registered trials
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