1. Universidad Antonio Nariño
  2. Trabajos de grado
  3. Pregrado
  4. Bioquímica
Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.uan.edu.co/handle/123456789/1496
Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.contributor.advisorMalagon Bernal, Edwin Andres-
dc.creatorCandela Londoño, Maria Fernanda-
dc.date.accessioned2021-02-18T18:45:08Z-
dc.date.available2021-02-18T18:45:08Z-
dc.date.created2020-11-20-
dc.identifier.urihttp://repositorio.uan.edu.co/handle/123456789/1496-
dc.descriptionInternaes_ES
dc.description.abstractInhibition of pancreatic lipase with Orlistat was used to show the correlation between experimental procedures and computational simulations. Both methods are important to understand the kinetics and the inhibition mechanism, and they complement each other in terms of the scope of the results obtained.The enzymatic activity of porcine pancreatic lipase was evaluated by determining kinetic parameters, such as the Michaelis constant- Menten and maximum speed, values corresponding to 61mM and 74µM / min, respectively. Orlistat inhibition tests were performed to obtain Lineweaver-Burk and Dixon graphs, complementary tools with which competitive inhibition was determined. In addition, a molecular coupling was included, to visualize the enzyme-Orlistat binding, along with a lipase sequence analysis to compare the structure of the enzyme in different organisms.es_ES
dc.description.sponsorshipOtroes_ES
dc.description.tableofcontentsLa inhibición de la lipasa pancreática con Orlistat se utilizó para mostrar la correlación entre procedimientos experimentales y simulaciones computacionales. Ambos métodos son importantes para entender la cinética y el mecanismo de inhibición, y se complementan en cuanto al alcance de los resultados obtenidos La actividad enzimática de la lipasa pancreática porcina se evaluó con la determinación de los parámetros cinéticos, tales como la constante de Michaelis-Menten y la velocidad máxima, valores que corresponden a 61mM y 74µM/min, respectivamente. Los ensayos de inhibición con Orlistat se realizaron para obtener las gráficas de Lineweaver-Burk y Dixon, herramientas complementarias con las que se determinó una inhibición competitiva. Además, se incluyó un acoplamiento molecular, para visualizar la interacció enzima-Orlistat, junto con un análisis de secuencias de lipasas para comparar la estructura de la enzima en diferentes organismos.es_ES
dc.language.isospaes_ES
dc.publisherUniversidad Antonio Nariñoes_ES
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 Estados Unidos de América*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectOrlistat, lipasa, inhibición, dockinges_ES
dc.titleInhibición de la lipasa porcina por orlistat: un ejercicio para entender la cinética enzimática, el mecanismo de acción del fármaco y la estructura enzimáticaes_ES
dc.publisher.programBioquímicaes_ES
dc.rights.accesRightsopenAccesses_ES
dc.type.spaTrabajo de grado (Pregrado y/o Especialización)es_ES
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersiones_ES
dc.source.bibliographicCitationHoude, A.; Kademi, A.; Leblanc, D. Lipases and Their Industrial Applications. An Overview. Appl. Biochem. Biotechnol. 2004, 118 (1-3), 155-170.es_ES
dc.source.bibliographicCitationFan, X.; Niehus, X.; Sandoval, G. Lipases as biocatalyst for biodiesel production. Methods Mol. Biol. 2012, 861, 471-483es_ES
dc.source.bibliographicCitationLia, S.; Pana, J.; Hua, X.; Zhangb, Y.; Gonga, D.; Zhang, G. Kaempferol inhibits the activity of pancreatic lipase and its synergistic effect with orlistat. J. Funct. Foods. 2020, 104041es_ES
dc.source.bibliographicCitationHeck, A.M.; Yanocski, J.A.; Calis, K.A. Orlistat, a New Lipase Inhibitor for the Management of Obesity. Pharmacotherapy. 2000, 20(3), 270-279es_ES
dc.source.bibliographicCitationDeng, H. Li, W. Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders. Acta Pharmac. Sin. B. 2020, 10(4):582-602es_ES
dc.source.bibliographicCitationKarup, S.; Sakharkar, P. Three-Dimensional Visualization of Kinase Inhibitors as Therapeutically Relevant Examples To Reinforce Types of Enzyme Inhibitors. J. Chem. Educ. 2019, 96 (2), 296-303es_ES
dc.source.bibliographicCitationRudnitskaya, A.; Török, B.; Török, D. Molecular Docking of Enzyme Inhibitors. Biochem. Mol. Biol. Edu. 2010, 38(4), 261-265.es_ES
dc.source.bibliographicCitationWhiteley, C. G. (2000). Enzyme kinetics: partial and complete uncompetitive inhibition. Biochemical Education, 28(3), 144-147.es_ES
dc.source.bibliographicCitationLocock, K., Tran, H., Codd, R., & Allan, R. (2015). Hands-On Approach to Structure Activity Relationships: The Synthesis, Testing, and Hansch Analysis of a Series of Acetylcholineesterase Inhibitors. Journal of Chemical Education, 92(10), 1745-1750es_ES
dc.source.bibliographicCitationLewis, D.; Liu, D. Direct Measurement of Lipase Inhibition by Orlistat Using a Dissolution Linked In Vitro Assay. Clin Pharmacol Biopharm. 2012, 1: 1000103.es_ES
dc.source.bibliographicCitationGuo, J.; Cheng, C.; Wanga, S.; Huang, X. A convenient test for lipase activity in aqueous-based solutions. Enzyme Microb. Technol. 2015, 71, 8-12es_ES
dc.source.bibliographicCitationChi, H.; Jain, H. Teaching Computing to STEM Students via Visualization Tools. Procedia Comput. Sci. 2011, 4, 1937-1943.es_ES
dc.source.bibliographicCitationHanwell, M.D.; Curtis, D.E.; Lonie, D.C.; Vandermeersch, T. Zurek, E.; Hutchison, G.R. Avogadro: an advanced semantic chemical editor, visualization, and analysis platform, J. Cheminfrmatics. 2012, 4, 1–17.es_ES
dc.source.bibliographicCitationGrosdidier, A.; Zoete, V.; Michielin, O. Swissdock a protein-small molecule docking web service based on EADock DSS. Nucleic Acids Res. 2011, 39, 270–277es_ES
dc.source.bibliographicCitationPettersen, E.; Goddard, T.; Huang, C. Couch, G., Greenblatt, D.; Meng, E. Ferrin, T. UCSF Chimera−A visualization system for exploratory research and analysis. J. Compt. Chem. 2005, 25, 1605-1612.es_ES
dc.source.bibliographicCitationBurlingham, B.; Widlanski, T. An Intuitive Look at the Relationship of Ki and IC50: A More General Use for the Dixon Plot. J. Chem. Educ. 2003, 80 (2), 214-218.es_ES
dc.source.bibliographicCitationLiu, T.; Liu, X.; Chen, Q.; Shi, Y. Lipase Inhibitors for Obesity: A Review. Biomed. Pharmacother. 2020, 128, 110314es_ES
dc.source.bibliographicCitationHaworth, N.; Martin, L. Biomolecules Come Alive: A Computer-Based Laboratory Experiment for Chemistry Students. J. Chem. Educ. 2018, 95 (12), 2256-2262.es_ES
dc.source.bibliographicCitationWorrall, A.; Bergstrom, P.; Young, D.; Wormald, S. Cahill, S.; Stewart, M. Benefits of Simulations as Remote Exercises During the COVID-19 Pandemic: An Enzyme Kinetics Case Study. J. Chem. Educ. 2020, in press.es_ES
dc.description.degreenameBioquímico(a)es_ES
dc.description.degreelevelPregradoes_ES
dc.publisher.facultyFacultad de Cienciases_ES
dc.description.funderProyecto FODEIND UTSA 2020es_ES
dc.description.notesPresenciales_ES
dc.creator.cedula1233893329es_ES
dc.publisher.campusBogotá - Circunvalar-
Aparece en las colecciones: Bioquímica

Ficheros en este ítem:
Fichero Tamaño  
2020AutorizacionAutores.pdf
  Restricted Access		75.89 kBVisualizar/Abrir  Request a copy
2020MariaFernandaCandelaLondoño.pdf552.5 kBVisualizar/Abrir
Mostrar el registro sencillo del ítem


Ver Estadísticas de uso



Este ítem está sujeto a una licencia Creative Commons Licencia Creative Commons Creative Commons