Antibodies targeting enzyme inhibition as potential tools for research and drug development

Antibodies have transformed biomedical research and are now being used for different experimental applications. Generally, the interaction of enzymes with their specific antibodies can lead to a reduction in their enzymatic activity. The effect of the antibody is dependent on its narrow i.e. the regions of the enzyme to which it is directed. The mechanism of this inhibition is rarely a direct combination of the antibodies with the catalytic site, but is rather due to steric hindrance, barring the substrate access to the active site. In several systems, however, the interaction with the antibody induces conformational changes on the enzyme that can either inhibit or enhance its catalytic activity. The extent of enzyme inhibition or enhancement is, therefore, a reflection of the nature and distribution of the various antigenic determinants on the enzyme molecule. Currently, the mode of action of many enzymes has been elucidated at the molecular level. We here review the molecular mechanisms and recent trends by which antibodies inhibit the catalytic activity of enzymes and provide examples of how specific antibodies can be useful for the neutralization of biologically active molecules.

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Bibliographic Details
Main Authors: Pérez de Lastra, José Manuel, Baca González, Victoria, González-Acosta, Sergio, Asensio Calavia, Patricia, Otazo-Pérez, Andrea, Morales-delaNuez, Antonio
Other Authors: Interreg MAC
Format: artículo de revisión biblioteca
Language:English
Published: Walter de Gruyter 2021-12-31
Subjects:Enzyme, inhibitor, antibody, disease, steric hindrance, allosteric,
Online Access:http://hdl.handle.net/10261/259913
http://dx.doi.org/10.13039/501100007757
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