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Title: Refinamiento de la mutación W107Rde la enzima KatG deMycobacterium tuberculosis y estudio de docking con Isoniazida
Author: Rodríguez Merchán, María
Director: Merino Arranz, David
Tutor: Fajardo, Emmanuel
Keywords: molecular docking
enzymes
Mycobacterium tuberculosis
refinement
Issue Date: 8-Jun-2021
Publisher: Universitat Oberta de Catalunya (UOC)
Abstract: W107R mutation of KatG (catalase-peroxidase) enzyme from Mycobacterium tuberculosis, this microorganism causes tuberculosis disease. KatG is an enzyme whose three-dimensional structure of its mutation is unknown. This enzyme is important in the microorganism, because it is responsible for activating the most widely used prodrug to alleviate the disease, Isoniazid, but actually there are problems of resistance to this drug, caused by mutations in KatG enzyme. Furthermore, it is important to study and understand the association of the drug with the enzymes through docking studies. This will help to elucidate the mechanisms to synthesize new molecules capable of controlling the disease. In this work, in silico techniques will be used for protein refinement (W107R mutation of M.tuberculosis KatG enzyme) This studies will be the first step to docking studies that ensure the reduction of resistance of isoniazid to tuberculosis disease. Through FoldX biomolecular modeling program and Autodock-Vina coupling studies, structural and binding differences between W107R and the non-mutated protein KatG have been verified, concluding possible escape mechanisms of the enzyme through mutations that lead to a lower energy of union and decrease of interactions.
Language: Spanish
URI: http://hdl.handle.net/10609/133253
Appears in Collections:Bachelor thesis, research projects, etc.

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