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    Home > Active Ingredient News > Antitumor Therapy > The Synthetic Routes of Infliximab

    The Synthetic Routes of Infliximab

    • Last Update: 2023-05-12
    • Source: Internet
    • Author: User
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    Infliximab is a chimeric monoclonal antibody used to treat a variety of autoimmune diseases, including Crohn's disease and ulcerative colitis.
    This medication works by binding to a specific protein, known as tumor necrosis factor-alpha (TNF-alpha), which is involved in the inflammatory response.
    Synthetic routes of Infliximab are various methods that are used to manufacture this medication in the chemical industry.
    In this article, we will discuss the various synthetic routes of Infliximab, as well as their advantages and disadvantages.


    1. Hybridoma Technology
      One of the first synthetic routes of Infliximab was through the use of hybridoma technology.
      In this process, a mouse with a specific antibody-producing B-cell is fused with a myeloma cell, creating a hybridoma cell that produces large amounts of monoclonal antibodies, such as Infliximab.
      This method is relatively simple and has been used for many years to produce monoclonal antibodies.
      However, it is not a cost-effective method for manufacturing Infliximab on a large scale due to the high cost of mouse maintenance and the low yield of monoclonal antibodies.
    2. Recombinant DNA Technology
      Recombinant DNA technology is another synthetic route of Infliximab that involves the use of genetic engineering to produce the medication.
      This method involves inserting the genes for the human antibody into a bacterial or yeast cell, which then produces the antibody.
      Recombinant DNA technology allows for the mass production of Infliximab and has become the most common method for manufacturing this medication.
      This method is reliable and cost-effective, providing more consistent quality compared to the hybridoma technology method.
    3. Fusion Proteins
      Fusion proteins are another synthetic route of Infliximab.
      In this method, the human antibody is fused with a non-antibody protein, such as a heterodimeric partner or a second antibody, to increase the stability and half-life of the medication.
      This method is less commonly used compared to the recombinant DNA technology method due to the challenges in expressing and isolating the fusion protein.
    4. Antibody Fragment
      The last synthetic route of Infliximab is through the use of antibody fragments, such as Fab or scFv.
      These fragments are smaller and less complex than the full-length antibody and can be manufactured using recombinant DNA technology.
      Antibody fragments have a lower risk of immunogenicity and are easier to produce than full-length antibodies, making them a promising alternative to traditional methods.

    Advantages and Disadvantages of Synthetic Routes of Infliximab


    Hybridoma technology provides a high concentration of monoclonal antibodies, but it is not cost-effective for large-scale production due to the high cost of maintaining mice and low yield of monoclonal antibodies.
    Recombinant DNA technology is cost-effective and allows for mass production of Infliximab, but it can be challenging to express and isolate the protein.
    Fusion proteins can increase the stability and half-life of the medication, but they are less commonly used due to the challenges in expressing and isolating the protein.
    Antibody fragments are a promising alternative to traditional methods due to their smaller size and lower risk of immunogenicity.


    In conclusion, there are several synthetic routes of Infliximab that are used in the chemical industry, including hybridoma technology, recombinant DNA technology, fusion proteins, and antibody fragments.
    Each method has its advantages and disadvantages, and the choice of method will depend on the specific needs of the manufacturer and patient.
    Regardless of the method used, it is essential that the final product is of high quality and meets all standards for safety and efficacy.


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