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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.
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