Protein misfolding

Research Group Marco Luciani: Protein Misfolding
Research Group: Protein Misfolding

Just like origamis, in order to elicit their physiological function, proteins must follow an exact sequence of folding regardless of localization, turnover and molecular size. In case this is not respected, protein can acquire erroneous spatial conformation by being folded in wrong ways and potentially eliciting cell stress. Luckily, cells are equipped with molecular machineries devoted in tagging, unfolding, refolding or degrade disarranged proteins (monomers). If these systems are overwhelmed, monomers will accumulate leading to the formation of oligomers and ultimately to amyloid fibers thus impairing cell, tissue and organ functions.  
This axiom called protein folding, in case of derangement, is the biological foundation of aging systems characterizing various chronic neurodegenerative diseases as Alzheimer’s dementia and it has been recently recognized as a driving mechanism of damage in a number of cardiovascular diseases.

Our group investigates a number of aspects related to protein misfolding in the cardiovascular system with a translational approach:

  • finding new therapeutic targets for protein misfolding in acute and chronic settings
  • identifying neglected proteins with amyloidogenic tendency
  • treating aging as a curable or a preventable condition
  • studying the systemic nature of Alzheimer’s as the archetype of misfolding
Protein misfolding illustration