Amyloidogenic proteins and prions are proteins that show specific structural features, and are generally linked to the development of several disorders, mainly neurodegenerative ones. However, recently has been discovered the amyloid nature as a critical specie to perform different physiological functions, where the long-term memory consolidation is included. In Aplysia, the protein responsible for this, which further comprises a prion-like behavior, corresponds to a specific isoform of CPEB protein, being in Drosophila its homologue Orb2.
In our laboratory, we are interested to go into details of the amyloidogenic pathway and to shed light about what makes an amyloid becomes toxic or functional, since they share the main part of their structural properties. To this end, we are focused in the study of neurotoxic proteins such as β-amyloid peptide and tau, α-synuclein, and polyQ expanded proteins, linked to the development of neurodegenerative disorders, such as Alzheimer's, Parkinson's and different spinocerebellar ataxias and Huntington, respectively. In addition, we analyze the functional amyloidogenesis of CPEB and Orb2. In order to reach this end, we perform analysis at different levels, from a single molecule approach, through cell cultures, and finally reaching the whole organism, to finally obtain a global and dissected vision of the complete process.