Binary Exo-Chiralities in the Peptide α-Helix Studied by Circular Dichroism

• Autores: Rebeca Gómez Ojea
• Directores de la Tesis: Javier Montenegro García (dir. tes.), Julian Bergueiro Álvarez (dir. tes.), Juan Granja Guillan (tut. tes.)
• Lectura: En la Universidade de Santiago de Compostela ( España ) en 2025
• Idioma: inglés
• Tribunal Calificador de la Tesis: Aitziber López Cortajarena (presid.), María Magdalena Cid Fernández (secret.), Marcos Daniel García Romero (voc.)
• Programa de doctorado: Programa de Doctorado en Ciencia y Tecnología Química por la Universidad de Santiago de Compostela y la Universidad de Vigo
• Calificación: Sobresaliente Cum Laude
• Materias:
  • Química
    • Bioquímica
      • Péptidos
    • Química macromolecular
      • Modificación de macromoléculas
    • Química orgánica
      • Estereoquímica y análisis conformacional
• Enlaces
  • Tesis en acceso abierto en: MINERVA
• Resumen

  • Biomacromolecules such as peptides are inherently chiral. Topological information displayed on its surface when folded into helical secondary conformations is key for functionality and assembly into high-order structures, with exo-helical topologies representing a superior level of chirality. The peptide helical backbone is a perfect template for studying exo-chiralities since their sequence-controlled synthesis allows to create tailored exo-helices based on repetition patterns, using circular dichroism for their study via chromophore functionalization. In this thesis, we have designed a map of elemental repetition patterns to unveil binary exo-chiralities of the -helix through individual contributions. Functionalization with different chromophores allowed to independently detect each exo-helix in the binary topology.