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    dc.contributor.authorGarcía Delgado, Cesar Sebastián.-
    dc.date.accessioned2024-07-02T15:52:49Z-
    dc.date.available2022-09-01-
    dc.date.available2024-07-02T15:52:49Z-
    dc.date.issued2022-
    dc.identifier.citationGarcía Delgado, C. S. (2022). Estudio computacional de la interacción del péptido amiloide de los islotes pancreáticos (hiapp) con membranas hidroperoxidadas [Trabajo de Grado Pregrado, Universidad de Pamplona]. Repositorio Hulago Universidad de Pamplona. http://repositoriodspace.unipamplona.edu.co/jspui/handle/20.500.12744/8907es_CO
    dc.identifier.urihttp://repositoriodspace.unipamplona.edu.co/jspui/handle/20.500.12744/8907-
    dc.descriptionPOPC (1-palmitoil-2-oleoil-sn-glicero-3-fosfocolina) es el fosfolípido más abundante en las células β del páncreas. Este lípido presenta una monoinsaturación en una de sus cadenas alifáticas, haciéndolo susceptible a la adición de un grupo hidroperóxido (R-OOH) a causa de la peroxidación lipídica ocasionada por el estrés oxidativo celular. Esta oxidación tiene varios efectos sobre las propiedades fisicoquímicas de la membrana alterando su composición y complejidad. Las células β tienen la función de secretar insulina y junto con ella la amilina, también conocida como el polipéptido amiloide de los islotes de Langerhans Humanos (hIAPP), principal componente de los depósitos amiloides encontrados en el páncreas de pacientes con diabetes tipo 2 (T2D). Hay evidencias que relacionan la oxidación lipídica con la formación de estructuras β-amiloides o estructuras oligoméricas intermediarias en hIAPP. Se cree que esto es debido a que los nuevos grupos de carga producto de la oxidación lipídica, mejorarían la interacción del péptido con la membrana. Mediante simulaciones por Dinámica Molecular (MD) se ha analizado la interacción de hIAPP con bicapas de fosfatidilcolina neutras e hidroperoxidadas (POPC y POPCOOH, respectivamente), usando el paquete de simulación Gromacs. Inicialmente se crearon dos modelos de bicapa monolipídicas para POPC y POPCOOH, analizando sus propiedades fisicoquímicas: área por lípidio, espesor, densidad y solvatación. Estabilizadas las bicapas, se agregó a hIAPP en la zona acuosa de la caja de simulación en cercanías a la superficie de la bicapa, evaluando la interacción péptido-bicapa durante 500 ns de simulación. Se analizaron las energías de interacción péptido-bicapa, la distancia del péptido al centro de bicapa, la formación de puentes de hidrógeno, además de la influencia de la bicapa en el contenido de estructura secundaria de hIAPP. Los resultados obtenidos indican que la hidroperoxidación lipídica aumenta el área por lípido, incrementando su solvatación, al tiempo que disminuye el grosor de la bicapa. Además, se favorece la interacción de hIAPP con los lípidos hidroperoxidados, debido a que el grupo R-OOH en la cadena alifática se ubica en la interfase apolar/polar de la bicapa. Así, la interacción primaria de hIAPP se observó inicialmente a través de su región N-terminal, favorecida por las interacciones electrostáticas. Con el paso del tiempo de simulación, el núcleo amiloidogénico (de características hidrofóbicas) ve favorecida sus interacciones de Van der Waals con la bicapa, al tiempo que aumenta su contenido de hélices-α.es_CO
    dc.description.abstractEl autor no proporciona la información sobre este ítem.es_CO
    dc.format.extent63es_CO
    dc.format.mimetypeapplication/pdfes_CO
    dc.language.isoeses_CO
    dc.publisherUniversidad de Pamplona - Facultad de Ciencias Básicas.es_CO
    dc.subjectDinámica Molecular.es_CO
    dc.subjecthIAPP.es_CO
    dc.subjectInteracción péptido bicapa.es_CO
    dc.subjectPeroxidación lipídica.es_CO
    dc.subjectPOPC.es_CO
    dc.titleEstudio computacional de la interacción del péptido amiloide de los islotes pancreáticos (hiapp) con membranas hidroperoxidadas.es_CO
    dc.typehttp://purl.org/coar/resource_type/c_7a1fes_CO
    dc.date.accepted2022-06-01-
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