ArticleIranian biomedical journal2018
Ofatumumab Monoclonal Antibody Affinity Maturation Through in silico Modeling
Article in Iranian biomedical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 27 citations in OpenAlex.
- Using Short Molecular Dynamics Simulations to Determine the Important Features of Interactions in Antibody-Protein Complexes.Proteins · 2025Article
- Emerging role of mucins in antibody drug conjugates for ovarian cancer therapy.Journal of ovarian research · 2024Review
- Anti-cancer peptide-based therapeutic strategies in solid tumors.Cellular & molecular biology letters · 2022Article
- A universal in silico V(D)J recombination strategy for developing humanized monoclonal antibodies.Journal of nanobiotechnology · 2022Article
- Ofatumumab and Granzyme B as immunotoxin against CD20 antigen.In silico pharmacology · 2022Article
- Atezolizumab and granzyme B as immunotoxin against PD-L1 antigen; an insilico study.In silico pharmacology · 2021Article
- Design of an engineered ACE2 as a novel therapeutics against COVID-19.Journal of theoretical biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Ofatumumab, an anti-CD20 mAb, was approved in 2009 for the treatment of chronic lymphocytic leukemia. This mAb acts through immune-mediated mechanisms, in particular complement-dependent cytotoxicity and antibody-dependent cellular cytotoxicity by natural killer cells as well as antibody-dependent phagocytosis by macrophages. Apoptosis induction is another mechanism of this antibody. Computational docking is the method of predicting the conformation of an antibody-antigen from its separated elements. Validation of the designed antibodies is carried out by docking tools. Increased affinity enhances the biological action of the antibody, which in turn improves the therapeutic effects. Furthermore, the increased antibody affinity can reduce the therapeutic dose of the antibody, resulting in lower toxicity and handling cost. Methods: Considering the importance of this issue, using in silico analysis such as docking and molecular dynamics, we aimed to find the important amino acids of the Ofatumumab antibody and then replaced these amino acids with others to improve antibody-binding affinity. Finally, we examined the binding affinity of antibody variants to antigen. Results: Our findings showed that variant 3 mutations have improved the characteristics of antibody binding compared to normal Ofatumumab antibodies. Conclusion: In the present study, the designed anti-CD20 antibodies showed to have potential for improved affinity compared to commercial Ofatumumab.
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Registered trials
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