Estudio in silico de la interacción entre la insulina glargina y el receptor híbrido IR/IGF1R

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dc.contributor.advisorGómez Alegría, Claudio Jaimespa
dc.contributor.advisorGonzález Beltrán, Martha Margaritaspa
dc.contributor.authorArévalo Corredor, Luis Fernandospa
dc.contributor.cvlacAREVALO CORREDOR, LUIS FERNANDOspa
dc.contributor.researchgroupUnimolspa
dc.date.accessioned2024-02-05T20:43:16Z
dc.date.available2024-02-05T20:43:16Z
dc.date.issued2023-12
dc.descriptionilustraciones a color, diagramasspa
dc.description.abstractIntroducción: La insulina glargina se une a receptores de la familia IR-IGF1R, incluyendo al receptor de insulina (IR) y de IGF1 (IGF1R) que regulan metabolismo, división y diferenciación celular. Las células también expresan receptores híbridos IR/IGF1R que se han asociado con efectos mitogénicos in vitro. Aunque existe bastante información de la estructura y mecanismo de activación de los receptores IR e IGF1R, se conoce muy poco del reconocimiento y activación de los receptores híbridos. Objetivo: Mediante acercamiento In silico, proponer un hipotético modelo estructural del receptor híbrido IR/IGF1R y estudiar la interacción glargina-receptor en dicho modelo. Metodología: Se utilizaron herramientas bioinformáticas (Swiss-model, ClusPro, LZerD y HADDOCK) para construir modelos computacionales del receptor híbrido. Resultados: Se obtuvo un total de 182 modelos computacionales del receptor híbrido IR/IGF1R, seleccionado finalmente un modelo del receptor libre (sin glargina o Apo-receptor) y otro del receptor con glargina unida (Holo-receptor), y se analizaron las interacciones ligando-receptor involucradas. Las afinidades teóricas calculadas (Kd) para el complejo glargina-receptor presentaron valores de 1.4 y 7.0 nM para los protómeros IR e IGF1R, respectivamente, lo que concuerda relativamente bien con datos experimentales reportados por otros autores. Conclusiones: Se proponen dos modelos computacionales de la estructura 3D del receptor híbrido IR/IGF1R, uno en su estado apo-y otro en su estado holo-receptor, describiendo las interacciones ligando-receptor encontradas. (Texto tomado de la fuente)spa
dc.description.abstractIntroduction: Insulin glargine binds to the IR-IGF1R family of receptors, which include the insulin receptor (IR) and the IGF1 receptor (IGF1R) governing cell metabolism, cell division, and differentiation. Cells also express hybrid IR/IGF1R receptors that have been associated with mitogenic effects in vitro. Although there is considerable information on the structure and activation mechanism of IR and IGF1R receptors, very little is known about the recognition and activation of the hybrid receptors. Aims: Using an in silico approach, to propose a hypothetical structural model of the hybrid IR/IGF1R receptor and to study the glargine-receptor interaction in this model. Methods: Bioinformatics tools (Swiss-model, ClusPro, LZerD and HADDOCK) were used to build computational models of the hybrid receptor. Results: A total of 182 computational models of the hybrid IR/IGF1R receptor were obtained, finally selecting a model of the free receptor without glargine (Apo-receptor) and another of the receptor with glargine bound (Holo-receptor), and the ligand-receptor interactions involved were analyzed. The calculated theoretical affinities (Kd) for the glargine-receptor complex presented values of 1.4 and 7.0 nM for the IR and IGF1R protomers, respectively, which agrees relatively well with experimental data reported by other authors. Conclusions: Two computational models for the 3D structure of the hybrid IR/IGF1R receptor are proposed, one for its apo-and the other for its holo-receptor state, and we describe the ligand-receptor interactions found.eng
dc.description.degreelevelMaestríaspa
dc.description.degreenameMagíster en Ciencias Farmacéuticasspa
dc.description.methodsSe utilizaron herramientas bioinformáticas (Swiss-model, ClusPro, LZerD y HADDOCK) para construir modelos computacionales del receptor híbrido.spa
dc.description.researchareaFarmacología Molecularspa
dc.description.sponsorshipno aplicaspa
dc.format.extent125 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/85626
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 Farmacéuticasspa
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dc.relation.referencesZhang, L. I., & Skolnick, J. (1998). What should the Z-score of native protein structures be? Protein Science: A Publication of the Protein Society, 7(5), 1201. https://doi.org/10.1002/PRO.5560070515spa
dc.relation.referencesZhang, X., Yu, D., Sun, J., Wu, Y., Gong, J., Li, X., Liu, L., Liu, S., Liu, J., Wu, Y., Li, D., Ma, Y., Han, X., Zhu, Y., Wu, Z., Wang, Y., Ouyang, Q., & Wang, T. (2020). isualization of Ligand-Bound Ectodomain Assembly in the Full-Length Human IGF-1 Receptor by Cryo-EM Single-Particle Analysis. Structure, 28(5), 555-561.e4. https://doi.org/10.1016/J.STR.2020.03.007spa
dc.relation.referencesRuiter, R., Visser, L. E., P van Herk-Sukel, M. P., W Coebergh, J. W., Haak, H. R., Geelhoed-Duijvestijn, P. H., J M Straus, S. M., C Herings, R. M., Ch Stricker, B. H., & C Stricker, B. H. (2011). Risk of cancer in patients on insulin glargine and other insulin analogues in comparison with those on human insulin: results from a large population-based follow-up study. https://doi.org/10.1007/s00125-011-2312-4spa
dc.relation.referencesMannucci, E., Monami, M., Balzi, D., Cresci, B., Pala, L., Melani, C., Lamanna, C., Bracali, I., Bigiarini, M., Barchielli, A., Marchionni, N., & Rotella, C. M. (2010). Doses of Insulin and Its Analogues and Cancer Occurrence in Insulin-Treated Type 2 Diabetic Patients. Diabetes Care, 33(9), 1997. https://doi.org/10.2337/DC10-0476spa
dc.relation.referencesDaniecki, N. J., Bhatt, M. R., Yap, G. P. A., & Zondlo, N. J. (2022). Proline C−H Bonds as Loci for Proline Assembly via C−H/O Interactions. ChemBioChem, 23(24), e202200409. https://doi.org/10.1002/CBIC.202200409spa
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dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.licenseAtribución-NoComercial-SinDerivadas 4.0 Internacionalspa
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/spa
dc.subject.ddc610 - Medicina y salud::615 - Farmacología y terapéuticaspa
dc.subject.decsInsulina glarginaspa
dc.subject.decsInsulin glargineeng
dc.subject.decsReceptor IGF Tipo 1spa
dc.subject.decsReceptor, IGF Type 1eng
dc.subject.decsReceptor de insulinaspa
dc.subject.decsReceptor, insulineng
dc.subject.proposalGlarginaspa
dc.subject.proposalReceptor Insulinaspa
dc.subject.proposalReceptor IGF1Rspa
dc.subject.proposalDocking molecularspa
dc.subject.proposalReceptoresspa
dc.subject.proposalInsulin glargineeng
dc.subject.proposalInsulin receptoreng
dc.subject.proposalIGF1R receptoreng
dc.subject.proposalMolecular dockingeng
dc.subject.proposalReceptorseng
dc.subject.wikidataDocking (molecular)eng
dc.subject.wikidataAcoplamiento molecularspa
dc.titleEstudio in silico de la interacción entre la insulina glargina y el receptor híbrido IR/IGF1Rspa
dc.title.translatedIn silico study of the interaction between insulin glargine and the hybrid IR/IGF1R receptor.eng
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.professionaldevelopmentEstudiantesspa
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.fundernameNo aplicaspa

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