Proteomics and protein chemistry unit
Our research group, with a long-standing commitment to the chemistry and applications of bioactive peptides, has expanded its activity into the field of proteomics since we arrived at the UPF in 2002.
In peptide chemistry, we have enduring interests on peptide antibiotics and synthetic peptide vaccines. In the first area, we have designed lead structures with potent activities against bacteria, protozoa and fungi. Several of those peptides are currently being evaluated against clinical strains of Acinetobacter baumannii, Leishmania donovani and other pathogens. We are also interested in the structural dissection of complex, highly folded plant antimicrobial proteins (e.g., thionin, hevein) with a view to developing minimalist active versions of them. In the vaccine area, we have developed synthetic functional replicas of the main antigenic sites of foot-and-mouth disease virus that have been incorporated into different presentations as vaccine candidates.
In proteomics, we have started both intramural (UPF, IMIM, PRBB) and external collaborative projects focused, among other areas, on i) discovery of receptors for tissue-type plasminogen activator in pancreatic cells; with a view to elucidating the mechanisms of mitogenic signaling by this protein ii) characterization of post-translational modifications resulting from oxidative stress in amyloidoses and other conditions; iii) identification of phenotypes selected by Bcl-xL over-expression in breast cancer cells that in vivo enhance the ubiquity of clinical metastasis; iv) identification of proteins characteristic of the resistance patterns of Acinetobacter baumannii multi-resistant strains associated to nosocomial infections.