Barbara Lelj Garolla Di Bard

I am interested in the role that molecular chaperones have in supporting treatment resistant prostate cancer.  In particular, I work on the intracellular small HspB1 (Hsp27) and on the only known extracellular chaperone, Clusterin. My research focuses on understanding the biophysical properties of these molecules in solution with the final aim of designing effective drug screenings. Moreover, I look for solution conditions optimal for crystal growth and for other techniques (NMR and EM) that can be used for three dimensional structure determinations.

The main technique I use to characterize protein self-association is analytical ultracentrifugation, which is very powerful in obtaining oligomerization profiles in a vast number of conditions. I also use protein purification, chaperone assays, various types of spectroscopy and site-directed mutagenesis to understand what role each protein domain or conserved residues have for protein activity.

I use the knowledge acquired from my studies to develop effective drug screening for these non-enzymatic proteins.