Antibody-based therapies have emerged as powerful tools in the fight against cancer, providing targeted treatment options with reduced side effects. To further enhance their efficacy, researchers have been exploring the use of drug delivery systems (DDS) for the controlled release of antibodies. DDS would produce various benefits in drug efficacy, including improved convenience, reduced toxicity, and enhanced treatment outcomes.1 With the advancement of nanotechnology and increasing focus on antibody-related dosage forms, the development of advanced antibody delivery systems holds promise for cancer patients.
Typically, antibody-based drugs are administered through intravenous routes, although there are risks with infusion-related reactions. To improve patient medication convenience, DDSs controlled release may use strategies such as subcutaneous injections, local depot formulations, inhalation powders, and oral systems.2 Another example are hydrogels, which studies have shown to be a potential DDS, controlling the release of antibody-streptavidin conjugates from the agarose-desthiobiotin hydrogels via controlled dissolution of sparingly soluble biotin derivatives.3
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Chen, Z., Kankala, R. K., Yang, Z., Li, W., Xie, S., Li, H., Chen, Z., & Zou, L. (2022). Antibody-based drug delivery systems for cancer therapy: Mechanisms, challenges, and prospects. Theranostics, 12(8), 3719-3746. https://doi.org/10.7150/thno.72594
Ibeanu, N., Egbu, R., Onyekuru, L., Javaheri, H., Khaw, P. T., Williams, G. R., Brocchini, S., & Awwad, S. (2020). Injectables and Depots to Prolong Drug Action of Proteins and Peptides. Pharmaceutics, 12(10). https://doi.org/10.3390/pharmaceutics12100999
Huynh, V., & Wylie, R. G. (2018). Competitive Affinity Release for Long-Term Delivery of Antibodies from Hydrogels. Angewandte Chemie International Edition, 57(13), 3406-3410. https://doi.org/10.1002/anie.201713428
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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