Avances y desafíos en la formulación de anticuerpos monoclonales

La necesidad de innovar en el campo farmacéutico es de gran importancia, como en el caso del uso de anticuerpos monoclonales para el tratamiento de diferentes enfermedades; que han presentado aumento en los últimos tiempos, tales como cáncer, artritis reumatoide o COVID-19. La formulación de los ant...

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Autores:: Forero Romero, Mary Dayana

Tipo de recurso:: https://purl.org/coar/resource_type/c_7a1f

Fecha de publicación:: 2024

Institución:: Universidad El Bosque

Repositorio:: Repositorio U. El Bosque

Idioma:: spa

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dc.title.none.fl_str_mv	Avances y desafíos en la formulación de anticuerpos monoclonales
dc.title.translated.none.fl_str_mv	Advances and challenges in the formulation of monoclonal antibodies
title	Avances y desafíos en la formulación de anticuerpos monoclonales
spellingShingle	Avances y desafíos en la formulación de anticuerpos monoclonales Anticuerpo monoclonal Formulación Calidad Administración Avances Desafíos 615.19 Monoclonal antibody Formulation Quality Administration Advances Challenges
title_short	Avances y desafíos en la formulación de anticuerpos monoclonales
title_full	Avances y desafíos en la formulación de anticuerpos monoclonales
title_fullStr	Avances y desafíos en la formulación de anticuerpos monoclonales
title_full_unstemmed	Avances y desafíos en la formulación de anticuerpos monoclonales
title_sort	Avances y desafíos en la formulación de anticuerpos monoclonales
dc.creator.fl_str_mv	Forero Romero, Mary Dayana
dc.contributor.advisor.none.fl_str_mv	Jiménez Cruz, Ronald Andrés Ariza Márquez, Yeimy Viviana
dc.contributor.author.none.fl_str_mv	Forero Romero, Mary Dayana
dc.subject.none.fl_str_mv	Anticuerpo monoclonal Formulación Calidad Administración Avances Desafíos
topic	Anticuerpo monoclonal Formulación Calidad Administración Avances Desafíos 615.19 Monoclonal antibody Formulation Quality Administration Advances Challenges
dc.subject.ddc.none.fl_str_mv	615.19
dc.subject.keywords.none.fl_str_mv	Monoclonal antibody Formulation Quality Administration Advances Challenges
description	La necesidad de innovar en el campo farmacéutico es de gran importancia, como en el caso del uso de anticuerpos monoclonales para el tratamiento de diferentes enfermedades; que han presentado aumento en los últimos tiempos, tales como cáncer, artritis reumatoide o COVID-19. La formulación de los anticuerpos monoclonales enfrenta desafíos para mantener su estabilidad y calidad. En este documento según sus resultados se reconocen los posibles inconvenientes que presentan en el proceso de formulación, la selección correcta de excipientes, las incompatibilidades que pueden presentarse, posibles vías de administración y los estudios que buscan innovación, siempre buscando el bienestar del paciente. La presencia de un excelente vehículo de administración y un desarrollo riguroso permiten optimizar la efectividad de los anticuerpos monoclonales, garantizando su seguridad y eficacia a lo largo del tiempo, lo que es fundamental para mejorar la calidad de vida de los pacientes.
publishDate	2024
dc.date.accessioned.none.fl_str_mv	2024-11-20T02:03:45Z
dc.date.available.none.fl_str_mv	2024-11-20T02:03:45Z
dc.date.issued.none.fl_str_mv	2024-10
dc.type.coar.fl_str_mv	http://purl.org/coar/resource_type/c_7a1f
dc.type.local.none.fl_str_mv	Tesis/Trabajo de grado - Monografía - Pregrado
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dc.identifier.uri.none.fl_str_mv	https://hdl.handle.net/20.500.12495/13260
dc.identifier.instname.spa.fl_str_mv	Universidad El Bosque
dc.identifier.reponame.spa.fl_str_mv	reponame:Repositorio Institucional Universidad El Bosque
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url	https://hdl.handle.net/20.500.12495/13260
identifier_str_mv	Universidad El Bosque reponame:Repositorio Institucional Universidad El Bosque repourl:https://repositorio.unbosque.edu.co
dc.language.iso.fl_str_mv	spa
language	spa
dc.relation.references.none.fl_str_mv	[1] Y. Cui, P. Cui, B. Chen, S. Li, y H. Guan, “Monoclonal antibodies: formulations of marketed products and recent advances in novel delivery system”, el 3 de abril de 2017, Taylor and Francis Ltd. doi:10.1080/03639045.2017.1278768. [2] J. F. Flores Ramírez, H. García Bernal, E. Ulises, M. León, C. Ulises, y I. Martínez, “Monoclonal antibodies in medicine”, 11, pp. 25–28, 2019, [En línea]. Disponible en: https://repository.uaeh.edu.mx/revistas/index.php/tepexi/issue/archive [3] D. J. A Crommelin Robert D Sindelar Bernd Meibohm Editors Fundamentals, “Pharmaceutical Biotechnology”. [4] MINISTERIO DE SALUD Y PROTECCIÓNSOCIAL. "Por la cual se establecen los servicios y tecnologías de salud financiados con recursos de la Unidad de Pago por Capitación (UPC)". Resolución 2808 de 30 de diciembre 2022. [En línea]. Disponible en: https://www.minsalud.gov.co/Normatividad_Nuevo/Resolución%20No.%202808%20de%202022.pdf [5] C. Haeuser, P. Goldbach, J. Huwyler, W. Friess, y A. Allmendinger, “Excipients for Room Temperature Stable Freeze-Dried Monoclonal Antibody Formulations”, J Pharm Sci, vol. 109, núm. 1, pp. 807–817, 2020, doi: https://doi.org/10.1016/j.xphs.2019.10.016. [6] A. Tosstorff, T. Menzen, y G. Winter, “Exploring Chemical Space for New Substances to Stabilize a Therapeutic Monoclonal Antibody”, J Pharm Sci, vol. 109, núm. 1, pp. 301–307, 2020, doi: https://doi.org/10.1016/j.xphs.2019.10.057. [7] R. Torosantucci, D. Weinbuch, R. Klem, y W. Jiskoot, “Triethylenetetramine prevents insulin aggregation and fragmentation during copper catalyzed oxidation”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 84, núm. 3, pp. 464–471, 2013, doi: https://doi.org/10.1016/j.ejpb.2013.01.011. [8] P. Kheddo, A. P. Golovanov, K. T. Mellody, S. Uddin, C. F. van der Walle, y R. J. Dearman, “The effects of arginine glutamate, a promising excipient for protein formulation, on cell viability: Comparisons with NaCl”, Toxicology in Vitro, vol. 33, pp. 88–98, 2016, doi: https://doi.org/10.1016/j.tiv.2016.02.002. [9] S. Chabra et al., “288 Ixekizumab citrate-free formulation: Results from 2 clinical trials”, Journal of Investigative Dermatology, vol. 142, núm. 8, Supplement, p. S49, 2022, doi: https://doi.org/10.1016/j.jid.2022.05.296. [10] K. Izutsu, C. Yomota, H. Okuda, T. Kawanishi, T. W. Randolph, y J. F. Carpenter, “Impact of heat treatment on miscibility of proteins and disaccharides in frozen solutions”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 85, núm. 2, pp. 177–183, 2013, doi: https://doi.org/10.1016/j.ejpb.2013.05.004. [11] M. Jayaraman, P. M. Buck, A. Alphonse Ignatius, K. R. King, y W. Wang, “Agitation-induced aggregation and subvisible particulate formation in model proteins”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 87, núm. 2, pp. 299–309, 2014, doi: https://doi.org/10.1016/j.ejpb.2014.01.004. [12] C. Du et al., “Protection of therapeutic antibodies from visible light induced degradation: Use safe light in manufacturing and storage”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 127, pp. 37–43, 2018, doi: https://doi.org/10.1016/j.ejpb.2018.02.007. [13] B. Fongaro, V. Cian, F. Gabaldo, G. De Paoli, G. Miolo, y P. Polverino de Laureto, “Managing antibody stability: Effects of stressors on Ipilimumab from the commercial formulation to diluted solutions”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 176, pp. 54–74, 2022, doi: https://doi.org/10.1016/j.ejpb.2022.05.005. [14] J. Schuster, V. Kamuju, y R. Mathaes, “Fate of antibody and polysorbate particles in a human serum model”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 171, pp. 72–79, 2022, doi: https://doi.org/10.1016/j.ejpb.2021.12.005. [15] J. Schuster, C. E. Probst, H.-C. Mahler, S. Joerg, J. Huwyler, y R. Mathaes, “Assessing Particle Formation of Biotherapeutics in Biological Fluids”, J Pharm Sci, vol. 110, núm. 4, pp. 1527–1532, 2021, doi: https://doi.org/10.1016/j.xphs.2020.12.038. [16] Y. Yang et al., “Improving Trastuzumab’s Stability Profile by Removing the Two Degradation Hotspots”, J Pharm Sci, vol. 104, núm. 6, pp. 1960–1970, 2015, doi: https://doi.org/10.1002/jps.24435. [17] D. Schweizer et al., “Pharmacokinetics, biocompatibility and bioavailability of a controlled release monoclonal antibody formulation”, Journal of Controlled Release, vol. 172, núm. 3, pp. 975–982, 2013, doi: https://doi.org/10.1016/j.jconrel.2013.10.010. [18] A. Fayd’herbe De Maudave et al., “Intra-articular delivery of full-length antibodies through the use of an in situ forming depot”, Journal of Controlled Release, vol. 341, pp. 578–590, 2022, doi: https://doi.org/10.1016/j.jconrel.2021.12.010. [19] A. Portron et al., “A Phase I Study to Assess the Effect of Speed of Injection on Pain, Tolerability, and Pharmacokinetics After High-volume Subcutaneous Administration of Gantenerumab in Healthy Volunteers”, Clin Ther, vol. 42, núm. 1, pp. 108-120.e1, 2020, doi: https://doi.org/10.1016/j.clinthera.2019.11.015. [20] T. Arvinte et al., “Part 2: Physicochemical characterization of bevacizumab in 2 mg/mL antibody solutions as used in human i.v. administration: Comparison of originator with a biosimilar candidate”, J Pharm Biomed Anal, vol. 176, nov. 2019, doi: 10.1016/j.jpba.2019.112802. [21] J. O. Eloy, R. Petrilli, D. L. Chesca, F. P. Saggioro, R. J. Lee, y J. M. Marchetti, “Anti-HER2 immunoliposomes for co-delivery of paclitaxel and rapamycin for breast cancer therapy”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 115, pp. 159–167, 2017, doi: https://doi.org/10.1016/j.ejpb.2017.02.020. [22] F. Fathian kolahkaj, K. Derakhshandeh, F. Khaleseh, A. H. Azandaryani, K. Mansouri, y M. Khazaei, “Active targeting carrier for breast cancer treatment: Monoclonal antibody conjugated epirubicin loaded nanoparticle”, J Drug Deliv Sci Technol, vol. 53, p. 101136, 2019, doi: https://doi.org/10.1016/j.jddst.2019.101136. [23] H. Kouchakzadeh, S. A. Shojaosadati, F. Tahmasebi, y F. Shokri, “Optimization of an anti-HER2 monoclonal antibody targeted delivery system using PEGylated human serum albumin nanoparticles”, Int J Pharm, vol. 447, núm. 1, pp. 62–69, 2013, doi: https://doi.org/10.1016/j.ijpharm.2013.02.043. [24] A. Rollett et al., “HSA nanocapsules functionalized with monoclonal antibodies for targeted drug delivery”, Int J Pharm, vol. 458, núm. 1, pp. 1–8, 2013, doi: https://doi.org/10.1016/j.ijpharm.2013.10.022. [25] M. Sevieri et al., “Ferritin nanoconjugates guide trastuzumab brain delivery to promote an antitumor response in murine HER2 + breast cancer brain metastasis”, Pharmacol Res, vol. 196, p. 106934, 2023, doi: https://doi.org/10.1016/j.phrs.2023.106934. [26] C. Shi, F. Gao, X. Gao, y Y. Liu, “A novel anti-VEGF165 monoclonal antibody-conjugated liposomal nanocarrier system: Physical characterization and cellular uptake evaluation in vitro and in vivo”, Biomedicine & Pharmacotherapy, vol. 69, pp. 191–200, 2015, doi: https://doi.org/10.1016/j.biopha.2014.11.025. [27] S. Zalba et al., “Cetuximab-oxaliplatin-liposomes for epidermal growth factor receptor targeted chemotherapy of colorectal cancer”, Journal of Controlled Release, vol. 210, pp. 26–38, 2015, doi: https://doi.org/10.1016/j.jconrel.2015.05.271. [28] M. Gunawardana, M. M. Baum, T. J. Smith, y J. A. Moss, “An Intravaginal Ring for the Sustained Delivery of Antibodies”, J Pharm Sci, vol. 103, núm. 11, pp. 3611–3620, 2014, doi: https://doi.org/10.1002/jps.24154. [29] Y. Lin et al., “Nasal Spray of Neutralizing Monoclonal Antibody 35B5 Confers Potential Prophylaxis Against Severe Acute Respiratory Syndrome Coronavirus 2 Variants of Concern: A Small-Scale Clinical Trial”, Clinical Infectious Diseases, vol. 76, núm. 3, pp. E336–E341, 2023, doi: 10.1093/cid/ciac448. [30] M. Chen, H. Ouyang, S. Zhou, J. Li, y Y. Ye, “PLGA-nanoparticle mediated delivery of anti-OX40 monoclonal antibody enhances anti-tumor cytotoxic T cell responses”, Cell Immunol, vol. 287, núm. 2, pp. 91–99, 2014, doi: https://doi.org/10.1016/j.cellimm.2014.01.003. [31] M. Chen, H. Ouyang, S. Zhou, J. Li, y Y. Ye, “PLGA-nanoparticle mediated delivery of anti-OX40 monoclonal antibody enhances anti-tumor cytotoxic T cell responses”, Cell Immunol, vol. 287, núm. 2, pp. 91–99, 2014, doi: https://doi.org/10.1016/j.cellimm.2014.01.003. [32] R. Lee, “Formulación de Anticuerpo del Anti-factor de crecimiento endotelial vascular (VEGF) acuosa estable”, ΜΧ 2017009759 A, 27/10/2017. [33] Y. Gokarn, T. Kamerzell, M. Li, M. Cromwell, H. Liu, “Formulación de anticuerpos”, US 9,226,961 B2, 05/ 01/2016. [34] H. Krause; L. Baust; M. Dickes., “Formulación de anticuerpos humanos para el tratamiento del TNF-ALFA asociado a trastornos”, US 2018/0339046 Al, 29/11/2018. [35] W. Cao, J. Li, X. Liu, “Formulación del Anticuerpo PD-1”, US 11,130,809 B2, 28/09/2021 [36] M. J. Page et al., “Declaración PRISMA 2020: una guía actualizada para la publicación de revisiones sistemáticas”, Revista Española de Cardiología (English Edition), vol. 74, núm. 9, pp. 790–799, sep. 2021, doi: 10.1016/J.REC.2021.07.010.
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spelling	Jiménez Cruz, Ronald AndrésAriza Márquez, Yeimy VivianaForero Romero, Mary Dayana2024-11-20T02:03:45Z2024-11-20T02:03:45Z2024-10https://hdl.handle.net/20.500.12495/13260Universidad El Bosquereponame:Repositorio Institucional Universidad El Bosquerepourl:https://repositorio.unbosque.edu.coLa necesidad de innovar en el campo farmacéutico es de gran importancia, como en el caso del uso de anticuerpos monoclonales para el tratamiento de diferentes enfermedades; que han presentado aumento en los últimos tiempos, tales como cáncer, artritis reumatoide o COVID-19. La formulación de los anticuerpos monoclonales enfrenta desafíos para mantener su estabilidad y calidad. En este documento según sus resultados se reconocen los posibles inconvenientes que presentan en el proceso de formulación, la selección correcta de excipientes, las incompatibilidades que pueden presentarse, posibles vías de administración y los estudios que buscan innovación, siempre buscando el bienestar del paciente. La presencia de un excelente vehículo de administración y un desarrollo riguroso permiten optimizar la efectividad de los anticuerpos monoclonales, garantizando su seguridad y eficacia a lo largo del tiempo, lo que es fundamental para mejorar la calidad de vida de los pacientes.PregradoQuímico FarmacéuticoThe need for innovation in the pharmaceutical field is of great importance, as in the case of the use of monoclonal antibodies for the treatment of different diseases, which have been increasing in recent times, such as cancer, rheumatoid arthritis or COVID-19. The formulation of monoclonal antibodies faces challenges to maintain their stability and quality. In this document, according to its results, the possible drawbacks presented in the formulation process, the correct selection of excipients, the incompatibilities that may arise, possible routes of administration and the studies that seek innovation, always looking for the patient's welfare, are recognized. The presence of an excellent administration vehicle and a rigorous development allow optimizing the effectiveness of monoclonal antibodies, guaranteeing their safety and efficacy over time, which is essential to improve the quality of life of patients.application/pdfAtribución-NoComercial-CompartirIgual 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-sa/4.0/Acceso abiertohttp:/purl.org/coar/access_right/c_abf2/http://purl.org/coar/access_right/c_abf2Anticuerpo monoclonalFormulaciónCalidadAdministraciónAvancesDesafíos615.19Monoclonal antibodyFormulationQualityAdministrationAdvancesChallengesAvances y desafíos en la formulación de anticuerpos monoclonalesAdvances and challenges in the formulation of monoclonal antibodiesQuímica FarmacéuticaUniversidad El BosqueFacultad de CienciasTesis/Trabajo de grado - Monografía - Pregradohttps://purl.org/coar/resource_type/c_7a1fhttp://purl.org/coar/resource_type/c_7a1finfo:eu-repo/semantics/bachelorThesishttps://purl.org/coar/version/c_ab4af688f83e57aa[1] Y. Cui, P. Cui, B. Chen, S. Li, y H. Guan, “Monoclonal antibodies: formulations of marketed products and recent advances in novel delivery system”, el 3 de abril de 2017, Taylor and Francis Ltd. doi:10.1080/03639045.2017.1278768.[2] J. F. Flores Ramírez, H. García Bernal, E. Ulises, M. León, C. Ulises, y I. Martínez, “Monoclonal antibodies in medicine”, 11, pp. 25–28, 2019, [En línea]. Disponible en: https://repository.uaeh.edu.mx/revistas/index.php/tepexi/issue/archive[3] D. J. A Crommelin Robert D Sindelar Bernd Meibohm Editors Fundamentals, “Pharmaceutical Biotechnology”.[4] MINISTERIO DE SALUD Y PROTECCIÓNSOCIAL. "Por la cual se establecen los servicios y tecnologías de salud financiados con recursos de la Unidad de Pago por Capitación (UPC)". Resolución 2808 de 30 de diciembre 2022. [En línea]. Disponible en: https://www.minsalud.gov.co/Normatividad_Nuevo/Resolución%20No.%202808%20de%202022.pdf[5] C. Haeuser, P. Goldbach, J. Huwyler, W. Friess, y A. Allmendinger, “Excipients for Room Temperature Stable Freeze-Dried Monoclonal Antibody Formulations”, J Pharm Sci, vol. 109, núm. 1, pp. 807–817, 2020, doi: https://doi.org/10.1016/j.xphs.2019.10.016.[6] A. Tosstorff, T. Menzen, y G. Winter, “Exploring Chemical Space for New Substances to Stabilize a Therapeutic Monoclonal Antibody”, J Pharm Sci, vol. 109, núm. 1, pp. 301–307, 2020, doi: https://doi.org/10.1016/j.xphs.2019.10.057.[7] R. Torosantucci, D. Weinbuch, R. Klem, y W. Jiskoot, “Triethylenetetramine prevents insulin aggregation and fragmentation during copper catalyzed oxidation”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 84, núm. 3, pp. 464–471, 2013, doi: https://doi.org/10.1016/j.ejpb.2013.01.011.[8] P. Kheddo, A. P. Golovanov, K. T. Mellody, S. Uddin, C. F. van der Walle, y R. J. Dearman, “The effects of arginine glutamate, a promising excipient for protein formulation, on cell viability: Comparisons with NaCl”, Toxicology in Vitro, vol. 33, pp. 88–98, 2016, doi: https://doi.org/10.1016/j.tiv.2016.02.002.[9] S. Chabra et al., “288 Ixekizumab citrate-free formulation: Results from 2 clinical trials”, Journal of Investigative Dermatology, vol. 142, núm. 8, Supplement, p. S49, 2022, doi: https://doi.org/10.1016/j.jid.2022.05.296.[10] K. Izutsu, C. Yomota, H. Okuda, T. Kawanishi, T. W. Randolph, y J. F. Carpenter, “Impact of heat treatment on miscibility of proteins and disaccharides in frozen solutions”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 85, núm. 2, pp. 177–183, 2013, doi: https://doi.org/10.1016/j.ejpb.2013.05.004.[11] M. Jayaraman, P. M. Buck, A. Alphonse Ignatius, K. R. King, y W. Wang, “Agitation-induced aggregation and subvisible particulate formation in model proteins”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 87, núm. 2, pp. 299–309, 2014, doi: https://doi.org/10.1016/j.ejpb.2014.01.004.[12] C. Du et al., “Protection of therapeutic antibodies from visible light induced degradation: Use safe light in manufacturing and storage”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 127, pp. 37–43, 2018, doi: https://doi.org/10.1016/j.ejpb.2018.02.007.[13] B. Fongaro, V. Cian, F. Gabaldo, G. De Paoli, G. Miolo, y P. Polverino de Laureto, “Managing antibody stability: Effects of stressors on Ipilimumab from the commercial formulation to diluted solutions”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 176, pp. 54–74, 2022, doi: https://doi.org/10.1016/j.ejpb.2022.05.005.[14] J. Schuster, V. Kamuju, y R. Mathaes, “Fate of antibody and polysorbate particles in a human serum model”, European Journal of Pharmaceutics and Biopharmaceutics, vol. 171, pp. 72–79, 2022, doi: https://doi.org/10.1016/j.ejpb.2021.12.005.[15] J. Schuster, C. E. Probst, H.-C. Mahler, S. Joerg, J. Huwyler, y R. Mathaes, “Assessing Particle Formation of Biotherapeutics in Biological Fluids”, J Pharm Sci, vol. 110, núm. 4, pp. 1527–1532, 2021, doi: https://doi.org/10.1016/j.xphs.2020.12.038.[16] Y. Yang et al., “Improving Trastuzumab’s Stability Profile by Removing the Two Degradation Hotspots”, J Pharm Sci, vol. 104, núm. 6, pp. 1960–1970, 2015, doi: https://doi.org/10.1002/jps.24435.[17] D. Schweizer et al., “Pharmacokinetics, biocompatibility and bioavailability of a controlled release monoclonal antibody formulation”, Journal of Controlled Release, vol. 172, núm. 3, pp. 975–982, 2013, doi: https://doi.org/10.1016/j.jconrel.2013.10.010.[18] A. 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Page et al., “Declaración PRISMA 2020: una guía actualizada para la publicación de revisiones sistemáticas”, Revista Española de Cardiología (English Edition), vol. 74, núm. 9, pp. 790–799, sep. 2021, doi: 10.1016/J.REC.2021.07.010.spaLICENSElicense.txtlicense.txttext/plain; charset=utf-82000https://repositorio.unbosque.edu.co/bitstreams/ed57e9b6-7703-4317-8276-641929727610/download17cc15b951e7cc6b3728a574117320f9MD52Anexo 1 Acta de aprobacion.pdfapplication/pdf516928https://repositorio.unbosque.edu.co/bitstreams/c3e7ee86-6d31-4927-afd6-984c42a6bc0b/download710a8abbfd4c096bdf3ec6221dd550d3MD58Carta de autorizacion.pdfapplication/pdf219954https://repositorio.unbosque.edu.co/bitstreams/dabed7a8-7fe5-4d68-8da5-9fbf8a7b752c/downloadb883a781973ce2368e88520985f562cdMD59ORIGINALTrabajo de grado.pdfTrabajo de grado.pdfapplication/pdf873101https://repositorio.unbosque.edu.co/bitstreams/47294a95-fd0a-4ade-b396-6053b86b95dc/downloadbc7516e6d30f2f04307ce0ea79bc2b19MD54CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8893https://repositorio.unbosque.edu.co/bitstreams/738fb708-168d-4b5b-8fcb-c2d9a92ec654/download5310bb89a00d5ead086944535cc857c4MD57TEXTTrabajo de grado.pdf.txtTrabajo de grado.pdf.txtExtracted texttext/plain69466https://repositorio.unbosque.edu.co/bitstreams/3f98670d-9001-4faa-9ff4-3e9651913129/download2aed3feb5dc58de962c684f969371bb6MD510THUMBNAILTrabajo de grado.pdf.jpgTrabajo de grado.pdf.jpgGenerated Thumbnailimage/jpeg5046https://repositorio.unbosque.edu.co/bitstreams/5eb8960b-b818-4dd3-ab53-b88a4392f664/download5bb8eae83235c4abbfb404d29a979636MD51120.500.12495/13260oai:repositorio.unbosque.edu.co:20.500.12495/132602024-11-20 03:04:42.49http://creativecommons.org/licenses/by-nc-sa/4.0/Atribución-NoComercial-CompartirIgual 4.0 Internacionalopen.accesshttps://repositorio.unbosque.edu.coRepositorio Institucional Universidad El Bosquebibliotecas@biteca.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