Mecanismo de acción de proteínas i péptidos antimicrobianos. Actividad bactericida de las ribonucleasas citotóxicas
- Autores: Marc Torrent Burgas
- Directores de la Tesis: Ester Boix i Borràs (dir. tes.), M. Victòria Noguès i Bara (codir. tes.)
- Lectura: En la Universitat Autònoma de Barcelona ( España ) en 2009
- Idioma: español
- Tribunal Calificador de la Tesis: Josep Vendrell Roca (presid.), Xavier Fernández Busquets (secret.), Marta Bruix Bayes (voc.)
- Materias:
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- Resumen
The project entitled "Mechanism of action of antimicrobial proteins and peptides. Bactericidal activity of cytotoxic ribonucleases" is centered in the study of cytotoxic ribonucleases, concretely eosinophil cationic protein (ECP) and ribonuclease 7.
This project has allowed an important insight in the bactericidal mechanism of action of the cytotoxic ribonucleases, both at the bacterial cell wall level and the cytoplasmic membrane.
In this line, a prediction algorithm has been developed to identify active regions in antimicrobial proteins. This method is able to identify the minimal regions implied in this activity.
Together, all these investigations have allowed to identify and characterize the ECP N-terminus as a minimal region capable to maintain both the protein cytotoxic properties and the interaction and membrane disruption capacities.
Moreover, using computational approximations, a potential heparin binding zone has been identified in ECP. This region may also be implied in its cytotoxic mechanism and could be important in the bacteria cell wall interaction in both, Gram -negative and Gram -positive bacteria.
In conclusion, all these results open an investigation window in the field of peptide synthesis and chemical engineering to obtain derived structures of the ECP N-terminus. This approach can lead to the development of peptide derived drugs, alternative or complementary to classical antibiotics, nowadays less effective due to appearance of resistance mechanisms in bacteria.
