Obtención de péptidos derivados de toxinas de origen animal con actividad biológica mediante un sistema recombinante y síntesis química

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dc.contributor.advisorVega Castro, Nohora Angélicaspa
dc.contributor.advisorRubiano Castellanos, Claudia Consuelospa
dc.contributor.authorRuíz-Moya, Miguel Ángelspa
dc.contributor.researchgroupGrupo de Investigación en Proteinas Gripspa
dc.date.accessioned2025-03-18T17:29:41Z
dc.date.available2025-03-18T17:29:41Z
dc.date.issued2024
dc.descriptionilustraciones, diagramas, fotografías a color, tablasspa
dc.description.abstractLa toxina BmK AGAP, proveniente del escorpión Buthus martensii Karsch, modula la función de diversos canales iónicos celulares, exhibiendo actividad antitumoral en distintas líneas celulares derivadas de tumores. Se ha identificado que los canales TRPC6 funcionales están sobreexpresados en diversos tipos de cáncer, lo que los convierte en posibles marcadores de malignidad. En este trabajo, mediante docking molecular utilizando AutoDock Vina, se estudió la interacción de la toxina BmK AGAP con el canal TRPC6. A partir de estos resultados, se diseñaron ocho péptidos, seleccionándose los cinco con mejor interacción (mayor energía de unión) con el canal. Tres de estos péptidos (MR-B1, MR-B2 y MR-B3) se obtuvieron mediante síntesis química en fase sólida, mientras que los dos restantes (Bmk17 y Bmk20) se seleccionaron para producción mediante expresión recombinante en E. coli. Posteriormente, se evaluó la citotoxicidad de los péptidos en diferentes líneas tumorales, y se llevó a cabo un análisis preliminar de apoptosis mediante la evaluación de la expresión de algunos genes. Por otro lado, en el Grupo de Investigación de Proteínas (GRIP) se ha estudiado el efecto neuroprotector in vitro de péptidos derivados de la toxina Conantoquina G, entre los que destacan EAR20 (activador positivo del receptor N-metil D-aspartato (rNMDA)) y EAR19 (actividad antagonista potente y selectiva). Debido a que es necesario validar estos efectos in vitro en el microambiente que rodea al tejido neuronal en modelos humano, se requiere disponer de una fuente continua de estos péptidos, por lo que se evaluó su obtención mediante expresión recombinante en E. coli (Texto tomado de la fuente).spa
dc.description.abstractThe toxin BmK AGAP, derived from the scorpion Buthus martensii Karsch, modulates the activity of various cellular ion channels. It exhibits analgesic properties and antitumor activity in several tumor-derived cell lines. Functional TRPC6 channels have been identified as overexpressed in multiple types of cancer, making them potential malignancy markers or therapeutic targets. This study evaluated molecular docking using AutoDock Vina to investigate the interaction between the BmK AGAP toxin and the TRPC6 channel. Based on these analyses, eight peptides were selected, and the five showing the best interaction (highest binding energy) with the channel were selected. Three of these peptides (MR-B1, MR-B2, and MR-B3) were obtained via solid-phase chemical synthesis, while the other two (Bmk17 and Bmk20) used a recombinant expression system in E. coli. Subsequently, the effect of peptides was studied on various tumor cell lines, and a preliminary analysis of apoptosis was carried out by assessing the expression of selected genes. Previous studies conducted by the Protein Research Group (GRIP) evaluated the in vitro neuroprotective effect of peptides derived from the Conantokin G toxin. Among these, EAR20 acted as a positive modulator of the N-methyl-D-aspartate receptor (rNMDA), while EAR19 exhibited potent and selective antagonist activity. Although the effects of these peptides have been demonstrated in vitro models, it remains essential to consider the microenvironment surrounding neuronal tissue in human models. Therefore, to maintain a continuous supply of these peptides, this study evaluated their production through recombinant expression in E. coli.eng
dc.description.degreelevelMaestríaspa
dc.description.degreenameMagister en Ciencias Químicaspa
dc.description.methodsLos péptidos fueron diseñados en el laboratorio de bioinformática del Grupo de Investigación en Proteínas (BioinfoGRIP) de la Universidad Nacional de Colombia, a partir de modificaciones en la secuencia completa del péptido BmK AGAP (Li et al., 2019), conocido por su interacción comprobada con canales de calcio, sodio y potasio. El diseño y la evaluación in silico de la interacción de este ligando con el dominio extracelular del canal de calcio TRPC6 se llevaron a cabo utilizando los programas AutoDock Vina® y Discovery Studio®, con el fin de determinar su potencial interacción con el receptor.spa
dc.description.researchareaProducción de péptidos derivados de toxinas animalesspa
dc.format.extent153 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.identifier.instnameUniversidad Nacional de Colombiaspa
dc.identifier.reponameRepositorio Institucional Universidad Nacional de Colombiaspa
dc.identifier.repourlhttps://repositorio.unal.edu.co/spa
dc.identifier.urihttps://repositorio.unal.edu.co/handle/unal/87686
dc.language.isospaspa
dc.publisherUniversidad Nacional de Colombiaspa
dc.publisher.branchUniversidad Nacional de Colombia - Sede Bogotáspa
dc.publisher.facultyFacultad de Cienciasspa
dc.publisher.placeBogotá, Colombiaspa
dc.publisher.programBogotá - Ciencias - Maestría en Ciencias - Químicaspa
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dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.licenseAtribución-NoComercial 4.0 Internacionalspa
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/spa
dc.subject.ddc570 - Biología::572 - Bioquímicaspa
dc.subject.ddc570 - Biología::571 - Fisiología y temas relacionadosspa
dc.subject.lembTOXINASspa
dc.subject.lembToxinseng
dc.subject.lembPEPTIDOSspa
dc.subject.lembPeptideseng
dc.subject.lembSINTESIS QUIMICAspa
dc.subject.lembChemical synthesiseng
dc.subject.lembBIOSINTESISspa
dc.subject.lembBiosynthesiseng
dc.subject.lembCITOTOXICIDAD POR MEDIACION CELULARspa
dc.subject.lembCell-mediated cytotoxicityeng
dc.subject.lembMUERTE CELULARspa
dc.subject.lembCell deatheng
dc.subject.lembESPECTROSCOPIA NUCLEARspa
dc.subject.lembNuclear spectroscopyeng
dc.subject.proposalBmk AGAPspa
dc.subject.proposalTRPC6, EARspa
dc.subject.proposalPéptidos recombinantesspa
dc.subject.proposalSíntesis química en fase sólidaspa
dc.subject.proposalExpresión génicaspa
dc.subject.proposalAntitumoralesspa
dc.subject.proposalRecombinant peptideseng
dc.subject.proposalSolid phase peptide synthesiseng
dc.subject.proposalGenic expressioneng
dc.subject.proposalAntitumoral peptideeng
dc.titleObtención de péptidos derivados de toxinas de origen animal con actividad biológica mediante un sistema recombinante y síntesis químicaspa
dc.title.translatedProduction of bioactive peptides derived from animal toxins using recombinant systems and chemical synthesiseng
dc.typeTrabajo de grado - Maestríaspa
dc.type.coarhttp://purl.org/coar/resource_type/c_bdccspa
dc.type.coarversionhttp://purl.org/coar/version/c_ab4af688f83e57aaspa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/masterThesisspa
dc.type.redcolhttp://purl.org/redcol/resource_type/TMspa
dc.type.versioninfo:eu-repo/semantics/acceptedVersionspa
dcterms.audience.professionaldevelopmentBibliotecariosspa
dcterms.audience.professionaldevelopmentEstudiantesspa
dcterms.audience.professionaldevelopmentInvestigadoresspa
dcterms.audience.professionaldevelopmentPúblico generalspa
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa

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Maestría en Ciencias - Química