An antibody is an immunoglobulin molecule which is activated, proliferated and differentiated into plasma cells by B cells, and which is synthesized and secreted by plasma cells and has a specific amino acid sequence and can specifically bind to the corresponding antigen. The emergence of antibodies has greatly helped doctors to cure diseases, and when it comes to antibodies, they have to think about antibody drugs.
Antibody discovery
In 1953, the British biochemist Frederick Sanger successfully analyzed the chemical structure of insulin, which is also a protein, and pointed out the direction for scientists to analyze the structure of antibodies. In 1963, Edelman and Rodney Robert Porter (Sanger's first Ph.D. student) combined the results of two years of research to propose a more mature antibody molecular model. In 1969, Edelman and Porter completed an amazing achievement at the time. They successfully measured more than 1,300 amino acid sequences of antibodies and were the largest protein molecules for determining amino acid sequences at that time. In 1976, Japanese scientist Ligen Chuanjin and colleagues found that the distribution of antibody light chain genes in embryonic cells that do not produce antibodies and in the production of antibody myeloma cells revealed that the antibody genes in embryonic cells are far apart, and the antibody genes in myeloma cells. Close to the distance, this finding indicates that the germ cells are redistributed during the development of immune cells.
The emergence of humanized antibodies
The human-mouse chimeric antibody means that the constant region of the murine antibody is replaced by the constant region of the human antibody, and the variable region sequence of the murine mAb is retained to form a so-called human mouse chimeric antibody. In the mid-1980s, researchers genetically engineered murine monoclonal antibodies to produce humanized antibodies.
Although the chimeric antibody can partially solve the rejection problem of the heterologous protein, the murine variable region may still induce the HAMA reaction and interfere with the therapeutic effect. Therefore, the emergence of CDR-grafted human antibodies has brought about a turn for the development of humanized antibody drugs. Based on the chimeric antibody, the CDR-grafted antibody further replaces the mouse source with the framework region (FR), and only retains three murine-derived CDRs, and the humanity can reach more than 90%. Studies have found that FRs with support are sometimes involved in antibody binding, reducing the affinity of antigen-antibody binding.
Antibody & antibody drug
Antibody research has undergone a relatively tortuous development process. After the slow development in the early 20th century, by the advent of monoclonal antibody technology in 1975, it has been highly valued by scholars in related fields and is widely used in the fields of immunity, medicine, cancer and cell biology. The first application of monoclonal antibody therapy was in 1982, when Karr applied an anti-idiotype monoclonal antibody to the treatment of B-cell lymphoma, and the study of therapeutic antibodies soon became a hot spot in the biopharmaceutical industry.
After years of development, antibody drugs have occupied an important position in the treatment of major diseases such as malignant tumors and autoimmune diseases. The development speed is impressive, and it is the highest compound rate of biopharmaceuticals.
Antibodies have gone through more than a hundred years of history from the initial animal polyclonal to the current fully human antibodies. As antibody engineering technology continues to grow, the range of applications for antibodies is becoming more widespread. Antibody-based gene therapy has also begun to emerge as an emerging clinical treatment. And more and more new antibody drugs approved by the US FDA are born. Today, with the development of biotechnology, biologics represented by monoclonal antibody drugs will become a new trend in the development of new drugs.
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