Estructura 3D de péptidos con potencial actividad Leishmanicida
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Rodríguez Pineda, Mario Andrés
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Resumen: En este trabajo se sintetizaron 7 péptidos llamados DM 1.1, DM 1.2, DM 1.3, DM 1.4 DM 1.5, DM 1.6 y DM1.7 análogos de DM 1 (ALWKTMLKKLGTMAL). DM 1 es un derivado de la dermaseptina S1 (ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ), a la cual se le ha encontrado actividad antiparasitaria. Los péptidos sintetizados fueron evaluados con-tra bacterias E. Coli (gram -), S. Aureus (gram +) y contra parásitos de L. Panamensis, encontrándose actividad biológica contra estos agentes patógenos cuando son tratados in vitro con DM 1.4 y DM 1.6. Haciendo uso de la espectroscopia RMN se pudieron determinar las conformaciones y la estructura 3D de los péptidos DM 1.4 y DM 1.6, quienes fueron los de la mayor actividad biológica, encontrando que para DM 1.4 la estructura del péptido es de tipo α-hélice entre los aminoácidos W2 y W12; y para el DM 1.6 esta conformación se da entre W6 y L15
Abstract: In this work 7 peptides called DM 1.1, DM 1.2, DM 1.3, DM 1.4, DM 1.5, DM 1.6 and DM1.7 were synthesized. The peptides are analogues of DM1 (ALWKTMLKKLGTMAL). The latter is a derivative of dermaseptin S1 (ALWKTMLKKLGTMALHAGKAAL-GAAADTISQGTQ), a larger peptide with antiparasitic activity. The peptides were synthe-sized and evaluated against E. Coli (gram -) and S. Aureus (gram +) bacteria and, L. Panamensis parasites. It was found that DM 1.4 and DM 1.6 display in vitro biological activity against these pathogens. The 3D structures of the DM 1.4 and DM 1.6 peptides, those ones with the largest biolog-ical activity, were solved using NMR spectroscopy. It was found that DM 1.4 forms an α-helix between amino acids W2 and W12, while DM 1.6 forms an alpha-helix between W6 and L15
Abstract: In this work 7 peptides called DM 1.1, DM 1.2, DM 1.3, DM 1.4, DM 1.5, DM 1.6 and DM1.7 were synthesized. The peptides are analogues of DM1 (ALWKTMLKKLGTMAL). The latter is a derivative of dermaseptin S1 (ALWKTMLKKLGTMALHAGKAAL-GAAADTISQGTQ), a larger peptide with antiparasitic activity. The peptides were synthe-sized and evaluated against E. Coli (gram -) and S. Aureus (gram +) bacteria and, L. Panamensis parasites. It was found that DM 1.4 and DM 1.6 display in vitro biological activity against these pathogens. The 3D structures of the DM 1.4 and DM 1.6 peptides, those ones with the largest biolog-ical activity, were solved using NMR spectroscopy. It was found that DM 1.4 forms an α-helix between amino acids W2 and W12, while DM 1.6 forms an alpha-helix between W6 and L15