ArticleThe journal of physical chemistry. B2023
Minimal Coarse-Grained Model for Immunoglobulin G: Diffusion and Binding under Crowding.
Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Lymphoid-Tissue-on-Chip Recapitulates Human Antibody Responses In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- IgG-Bridging-Seeded Synergistic Aggregation of SARS-CoV-2 Spikes Underlies Potent Neutralization by a Low-Affinity Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Size Sensitivity of Metabolite Diffusion in Macromolecular Crowds.Nano letters · 2024Article
- The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
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Abstract
Immunoglobulin G (IgG) is the most common type of antibody found in blood and extracellular fluids and plays an essential role in our immune response. However, studies of the dynamics and reaction kinetics of IgG-antigen binding under physiological crowding conditions are scarce. Herein, we develop a coarse-grained model of IgG consisting of only six beads that we find minimal for a coarse representation of IgG's shape and a decent reproduction of its flexibility and diffusion properties measured experimentally. Using this model in Brownian dynamics simulations, we find that macromolecular crowding affects only slightly the IgG's flexibility, as described by the distribution of angles between the IgG's arms and stem. Our simulations indicate that, contrary to expectations, crowders slow down the translational diffusion of an IgG less strongly than they do for a smaller Ficoll 70, which we relate to the IgG's conformational size changes induced by crowding. We also find that crowders affect the binding kinetics by decreasing the rate of the first binding step and enhancing the second binding step.
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