Protein aggregation and cytotoxicity: molecular, in vitro and in vivo biological studies
Descrizione: Studies on protein misfolding and aggregation have been attracting growing interest not only among protein chemists but also in the field of molecular medicine. Nevertheless scientists have devoted intensive studies to the comprehension of the molecular basis of protein misfolding diseases, many obscure points must be clarified before an effective therapy can be proposed. Therefore, projects aimed at developing new molecules able to interact specifically with those proteins involved in misfolding processes and stabilize their native conformation are of utmost importance. The aims of the present research activity is to understand of the molecular processes, as well as the biological effects, underlying protein misfolding thus emphasizing the pathological events that characterize the prion and Alzheimers diseases, diabetes and related retinopathies as well as cataracts. As regards Prion and Alzheimers diseases, clarifying the relationships connecting oxidative stress and metal assisted aggregation processes will contribute to the validation of the current hypothesis on the development of these diseases. Quantification and characterization of the molecular species (oligomers, protofibrils, etc.) responsible for neuronal injury will also demonstrate the existence of a connection between metal ion dyshomeostasis, aggregate morphologies, amyloid toxicity, and neurodegeneration. In this context, the detailed knowledge of the crucial steps of the aggregation process are important for the development of a new generation of bioconjugated antifibrillogenic molecules endowed with pluripotent activities
86 Records (83 escludendo Abstract e Conferenze). Impact factor totale: 337.377 (326.737 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 330.769 (323.834 escludendo Abstract e Conferenze).