Comment by Fabrizio Beltrametti ( Branduardi’s Lab )
Intrinsically disordered proteins (IDPs) are characterized by their ability to react to subtle environmental fluctuations by rapidly converting in alternative conformers. IDPs have drawn attention in the field of molecular pathology since they tend to form toxic or non-toxic aggregates and fibrils. The most famous disease-related IDPs include Aβ(1-42) [Alzheimer's disease (AD)], Tau (AD and tauopathy), α-synuclein (Parkinson's disease) and p53 (cancer). These IDP formation processes are often initiated by transient conformational changes in which the overall health status of living cells and the influence of external physico-chemical conditions play a crucial role.
Native Mass Spectrometry (native MS) can largely help the analyses of the transient events of conformational equilibrium of IDPs and folded proteins. Our TeCSBi second year student Greta Bianchi ( Brocca’s Lab ) is actively using native MS as a tool to elucidate the conformational equilibrium of IDPs and has recently presented her work in the IDPSIG & IDPseminars virtual congress held on September the 9th 2021. Greta focused her attention on two viral IDP protein fragments (measles virus N-tail, Hendra virus PNT4). Would that be the new frontier of study for viruses leaving long term effects on the human body?
Thank you, Greta, for your activity in this hot topic!
Find out more about the event here: https://ecbs2021.eu/
Hashtags: #BtBsPhD , #TeCSBi , #TeCSBiSpotlight , #Parkinson , #BranduardiLab_BtBs , #BroccaLab_BtBs