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

Author:

Pérez de la Lastra José Manuel1,Baca-González Victoria12,González-Acosta Sergio1,Asensio-Calavia Patricia12,Otazo-Pérez Andrea12,Morales-delaNuez Antonio1

Affiliation:

1. Biotechnology of macromolecules . Instituto de Productos Naturales y Agrobiología (IPNA-CSIC) , San Cristóbal de la Laguna, Tenerife , Spain

2. Escuela Doctorado y Estudios de Posgrado . Universidad de La Laguna (ULL) . C/ Pedro Zerolo, s/n. 38200. San Cristóbal de La Laguna. S/C de Tenerife , Spain

Abstract

Abstract 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

Publisher

Walter de Gruyter GmbH

Subject

Cellular and Molecular Neuroscience,General Biochemistry, Genetics and Molecular Biology,General Medicine

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