Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)García Contreras, Germán AntonioSilva Yate, Edith Vanessa2021-02-222021-02-222020-06-03http://repositorio.uan.edu.co/handle/123456789/1599Cancer diagnostic methods are currently based on glycosylated biomarkers such as Tn antigen and can be detected by lectin-based technologies such as biosensors. However, there is a limitation due to the lack of commercial availability of lectins that recognize these structures, in addition to the fact that low stability may occur in biosensors due to the layers of proteins associated with them. In the present work we analyzed peanut lectin (Arachis Hypogaea), together with other lectins from legumes belonging to the Fabaceae family such as Glycine max (PDB 4D69), Wisteria Floribunda (PDB 5KXB), Psophocarpus Tetragonolobus (PDB 2D3S), and Isolectin B4 Vicia Villosa (1N47); where, based on their characteristics, peptides were designed and modeled and analyzed by means of molecular docking tests. Twelve candidate peptides were obtained for the library, eleven of which come from the structural segmentation of our protein of interest Arachis Hypogaea and one obtained from the comparisons and alignments of all the fabaceous proteins. The peptides analyzed by molecular docking were considered stable, of adequate length, with energy properties similar to peanut lectin when coupled with the antigen Tn, being considered excellent candidates to be later synthesized and analyzed for possible cancer diagnostic methods.Los métodos de diagnóstico del cáncer actualmente se basan en biomarcadores que se encuentran glucosilados como lo es el antígeno Tn y pueden ser detectados por tecnologías basadas en lectinas como son los biosensores. Sin embargo, hay una limitación por la falta de disponibilidad comercial de lectinas que reconocen estas estructuras, además de que puede presentarse baja estabilidad en los biosensores por las capas de proteínas asociadas a este. En el presente se trabajo se analizó la lectina de maní (Arachis Hypogaea), en conjunto de otras lectinas de leguminosas pertenecientes la familia Fabaceae como Glycine max (PDB 4D69), Wisteria Floribunda (PDB 5KXB), Psophocarpus Tetragonolobus (PDB 2D3S), e Isolectina B4 Vicia Villosa (1N47); en donde basándose en sus características se diseñaron y modelaron péptidos los cuales fueron analizados por medio de pruebas de docking molecular. Se obtuvieron doce péptidos candidatos para la librería los cuales, once provienen de la segmentación estructural de nuestra proteína de interés Arachis Hypogaea y uno obtenido en las comparaciones y alineamientos de todas las proteínas fabáceas. 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