Anticorpos monoclonais
Data
2021-02-05
Tipo
Trabalho de conclusão de curso
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ISSN da Revista
Título de Volume
Resumo
Anticorpos monoclonais (mAbs) são moléculas de imunoglobulinas idênticas
produzidas para um antígeno específico. Anticorpos são estruturalmente compostos por 2 cadeias leves e 2 cadeias pesadas que contém o sítio de ligação ao antígeno e a região que se liga à receptores das células do sistema imunológico. O primeiro anticorpo monoclonal foi produzido em 1975 com a técnica de produção de hibridoma, onde há fusão de uma célula de mieloma com uma célula B de um animal previamente imunizado. Porém, anticorpos murinos apresentam diferenças em relação aos anticorpos humanos e, por isso, foram relatadas reações de hipersensibilidade e rápida eliminação do organismo, comprometendo sua função terapêutica. Desde então, várias técnicas surgiram com o objetivo de aumentar a segurança e eficácia do mAbs. Essas técnicas incluem: anticorpos humanizados e quiméricos, produzidos pela tecnologia de DNA recombinante, por Phage Display, ou animais transgênicos; e anticorpos monoclonais humanos, produzidos por tecnologia de célula B única. Atualmente, há mais de 80 anticorpos monoclonais aprovados para a clínica, sendo a maior parte deles para tratamento de doenças, como câncer. Neste trabalho, foi realizada revisão bibliográfica com o objetivo de identificar e discutir as principais técnicas para obtenção de anticorpos monoclonais e suas aplicações.
Monoclonal antibodies (mAbs) are identical immunoglobulin molecules produced for a specific antigen. Antibodies are structurally composed of 2 light chains and 2 heavy chains that contain the antigen binding site and the region that binds to immune cell receptors. The first monoclonal antibody was produced in 1975 with a hybridoma production technique, where a myeloma cell fuses with a B cell of a previously immunized animal. However, murines antibodies differ from humans antibodies and, therefore, hypersensitivity reactions and rapid elimination from the organism have been reported, compromising their therapeutic function. Since then, several techniques have emerged with the aim of increasing the safety and effectiveness of mAbs. These techniques include: humanized and chimeric antibodies, produced using recombinant DNA technology, by Phage Display, or transgenic animals; human monoclonal antibodies, produced by single B cell technology. Currently, there are more than 80 monoclonal antibodies approved for the clinic, most of them for the treatment of diseases, such as cancer. In this work, a bibliographic review was carried out with the objective of identifying and discussing the main techniques for obtaining monoclonal and its applications.
Monoclonal antibodies (mAbs) are identical immunoglobulin molecules produced for a specific antigen. Antibodies are structurally composed of 2 light chains and 2 heavy chains that contain the antigen binding site and the region that binds to immune cell receptors. The first monoclonal antibody was produced in 1975 with a hybridoma production technique, where a myeloma cell fuses with a B cell of a previously immunized animal. However, murines antibodies differ from humans antibodies and, therefore, hypersensitivity reactions and rapid elimination from the organism have been reported, compromising their therapeutic function. Since then, several techniques have emerged with the aim of increasing the safety and effectiveness of mAbs. These techniques include: humanized and chimeric antibodies, produced using recombinant DNA technology, by Phage Display, or transgenic animals; human monoclonal antibodies, produced by single B cell technology. Currently, there are more than 80 monoclonal antibodies approved for the clinic, most of them for the treatment of diseases, such as cancer. In this work, a bibliographic review was carried out with the objective of identifying and discussing the main techniques for obtaining monoclonal and its applications.