ResourcesBlogAntibody-Drug Conjugates: A New Frontier in Cancer Treatment
Antibody-Drug Conjugates: A New Frontier in Cancer Treatment
Biointron2024-01-20Read time: 1 min
Image credit: DOI: 10.1007/s00277-021-04599-5
Antibody-drug conjugates (ADCs) are typically composed of a monoclonal antibody (mAbs) covalently bonded to a biologically active cytotoxic drug via a chemical linker. The mAb can then bind to a specific target protein or receptor, allowing the delivery of the drug into the target cell.
This combination allows for a highly specific targeting and potent killing effect to achieve accurate and efficient elimination of target cells, without harming healthy cells. This is particularly desirable in treating cancer, as chemotherapy has poor specificity towards tumor tissues and has toxicities to healthy tissues.1
Although most developed ADCs are designed to treat cancer, ongoing research are attempting to use ADCs to treat different diseases such as atherosclerosis, bacteremia, and inflammatory diseases. Furthermore, development of bispecific ADCs, as well as combinations of ADCs with immunotherapy, are anticipated to produce more safe and efficacious therapies.2
At Biointron, we are dedicated to accelerating antibody discovery for the development of antibody-based drugs for various diseases. Our team of experts can provide customized solutions that meet your specific research needs. Contact us to learn more about our services and how we can help accelerate your research and drug development projects.
Fu, Z., Li, S., Han, S., Shi, C., & Zhang, Y. (2022). Antibody drug conjugate: The “biological missile” for targeted cancer therapy. Signal Transduction and Targeted Therapy, 7(1), 1-25. https://doi.org/10.1038/s41392-022-00947-7
Antibodies are versatile molecules that perform a range of effector functions, many of which engage different arms of the immune system. Their modes of action extend beyond simple antigen binding, enabling the activation of various immune mechanisms that lead to pathogen neutralization and clearance. These functions include blocking molecular interactions, activating the complement system, and linking the humoral immune response to cellular immune responses via Fc receptor engagement.
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In addition to isotypes and subtypes, antibodies exhibit genetic variation known as allotypes, which are polymorphic epitopes on immunoglobulins. These allotypic differences arise from allelic variations in immunoglobulin genes, causing certain antibody subtypes to differ between individuals or ethnic groups. The presence of these polymorphic forms can influence immune responses, particularly when an individual is exposed to a non-self allotype, potentially triggering an anti-allotype immune reaction.
In mammals, antibodies are classified into five major isotypes: IgA, IgD, IgE, IgG, and IgM. Each isotype is defined by the heavy chain it contains: alpha (IgA), delta (IgD), epsilon (IgE), gamma (IgG), or mu (IgM). These structural differences in the heavy chains determine the antibody's function, tissue localization, and role in the immune response. Furthermore, antibody light chains fall into two classes—kappa and lambda—with kappa being more common, though both exhibit similar functions despite differences in sequence.
