CONICET Posdoctoral fellow
Director: M. Soledad Celej
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.
For this purpose, we will carry out chemical denaturing studies to obtain the first quantitative determination of the conformational stability of FapC amyloid, offering a physicochemical view of its potential protective role in bacterial ecosystems. In addition, we will determine role of electrostatic interactions in stabilizing such structure, which will be useful for building a molecular model of its fibrillar organization.