Research Focus: - Amyloidogenic diseases are characterized by misfolding, aggregation and accumulation of proteins inside or outside cells (also termed plaques). Amyloidogenic proteins initiate a cascade of deleterious pathophysiological sequelae that eventually culminate in cellular death. Increasing evidence indicates that the self-assembly of proteins is often associated with the molecular events leading to neuronal death in a range of neurodegenerative diseases,including Alzheimer's disease and Parkinson's disease. My research aims to use robust molecular screens to identify novel small-molecule inhibitors, including bioactive compounds from terrestrial and marine plants, that would be able to prevent amyloid aggregates from permeabilizing biomembranes. We are currently studying amyloid-beta peptide and alpha-synuclein, but hope to include other amyloid proteins in the future. With the help of our collaborators, we have used fluorescence correlation spectroscopy, liposome assays and electrophysiological methods, among others. We also use the structural diversity of natural compounds to establish structure-activity relationships for small-molecule inhibitors. In this regard, in the future we are interested in introducing computational molecular modeling techniques to assist in drug discovery.
International Collaborators: - Centre for Neuropathology and Prion Research, Ludwig-Maximilians-University, Munich, Germany. - Deutsches Zentrum fur Neurodegenerative Erkrankungen (DZNE), Munich, Germany - Research Centre on the Molecular Basis of Neurodegenerative Diseases, University of Florence, Italy.
Professional Affiliations: - Member of the American Physiological Society - Member of the American Chemical Society - Member of the European/International Society for Neurochemistry