3 July, 2015 – Aging, and many diseases such as cystic fibrosis, deep atherosclerosis, sepsis, asthma and Parkinson’s disease… Our proteins undergo a process called oxidative halogenation in which some hydrogen atoms are replaced by halogen ones, especially bromine and chlorine. Although there is a direct correlation between the two phenomena, it is still unclear the mechanism whereby halogenation induces a change in the three-dimensional structure of proteins and their functions, leading to aging or disease outbreaks. A group of Italian researchers (from the Politecnico di Milano and University of Salento) and Finland (Aalto University and VTT-Technical Research Centre), coordinated by Professor Pierangelo Metrangolo of the Politecnico di Milano, took a step forward in understanding this mechanism. They were able to demonstrate that the introduction of an iodine atom in a peptide sequence greatly accelerates its ability to self-assembly into amyloid fibrils, typical of some pathological states such as Alzheimer’s disease. This finding was published in Nature Communications, after only two years since the beginning of the project funded by the European Research Council (ERC) “Folding with Halogen Bonding”, born with the aim to elucidate the mechanisms of the effects of protein halogenation. (Red)
