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Integrantes

SIRI, Macarena

Becaria posdoctoral de CONICET
Directora: M. Soledad Celej
E-Mail: maca.siri@gmail.com

Tema de Posdoctorado

Estabilidad conformacional del amiloide funcional FapC del patógeno oportunista Pseudomonas aeruginosa
Las proteínas pueden auto-ensamblarse en amiloides, nanoestructuras fibrilares remarcablemente estables postuladas como el estado conformacional de minina energía accesible a toda cadena peptídica. Si bien fueron descubiertos en un contexto patológico, cada vez |más evidente que la naturaleza aprovecha las notables propiedades de estas nanoestructuras con fines funcionales. FapC es el nuevo amiloide funcional identificado en Pseudomonas confiriéndole un fenotipo agregativo y adherente con mayor tendencia a formar biofilm, el cual le confiere robustez mecánica y resistencia a estresores ambientales.

Posdoctoral Topic

Confomational stability of FapC, a novel functional amyloid from the opportunistic pathogen Pseudomona aeruginosa
Proteins can self-assemble into a minimum-energy conformational fibrillar structure known as amyloid. Although originally discovered in the context of human diseases, recent studies indicate that different organisms use amyoloids for functional purposes. FapC is the new functional amyloid recently identified in Pseudomonas. This amyloid not only acts as an adherent and aggregation factor in the bacteria biofilm, but also gives mechanical robustness and resistance against environmental stressors. This project is aimed at understanding the physicochemical basis of the adoption and maintenance of the fibrillar structure of the FapC functional amyloid of P. aeruginosa, an opportunistic pathogen associated with chronic and pulmonary infections. We will evaluate the conformational stability of FapC amyloid and determine the role of electrostatic interactions in stabilizing such structure.