Understanding prion peptide fibril-induced aggregation of prion protein





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.