|Call||Mutual funds Taiwan – Latvia – Lithuania, 2016|
|Implementation period||01.01.2017. – 31.12.2019.|
|Project partners||Institute of Biological Chemistry, Academia Sinica, Taiwan
Latvian Institute of Organic Synthesis, Latvia
Vilnius University, Lithuania
|Leader of Latvian team||Prof. Dr. Edvards Liepiņš|
|Total costs||202 500 EUR|
|Costs for Latvian partner||67 500 EUR|
Prion-like spreading may be employed in a number of fatal neurodegenerative disorders, including such as Alzheimer’s and Parkinson’s diseases. Understanding all possible mechanisms of such spreading would be a big step towards curing these diseases.
Recent work showed that prion protein aggregation can be induced by short peptides. It seems that either structure of peptide-induced prion protein aggregates (piPrP) or the mechanism of its formation is different from the current knowledge in the field.
We propose a comprehensive study of piPrP structure, starting from low resolution methods as Fourier transform infrared (FTIR) spectrometry and proteinase K (PK) resistance studies, but focusing on medium and high-resolution methods in hydrogen exchange mass spectrometry (HXMS), electron spin resonance spectrometry (ESR), and solid-state nuclear magnetic resonance spectroscopy (ssNMR). High resolution structure will lead to the ultimate goal of our research – getting deeper into mechanisms of prion-like self-replication of amyloid fibrils.