Oleksandra KuryshevaPhD student

Soluble amyloid-β 42 (Aβ42) oligomers play a major role in the pathogenesis of Alzheimer`s disease (AD) as the most cytotoxic Aβ peptide species. As some studies showed, lipid environments promote Aβ aggregation under certain conditions. However, the underlying mechanism through which lipids, including those of the cell membrane, affect Aβ structure remains unclear.

Here, we use time-resolved infrared spectroscopy to investigate Aβ42 aggregation behaviour in membrane-mimetic environments under physiological conditions in vitro. This technique is widely used for studying peptide secondary structure by the changes of absorption in the amide I region. Coupling the instrument with temperature control allows us to monitor the whole oligomerization process of Aβ42 by simultaneously collecting spectral data. We are also planning to employ site-specifically 13C-labelled peptides to reveal lipid-induced structural changes with residue-level resolution, which is a unique approach for studying lipid-peptide interaction. 

Overall, understanding the fundamental process of Aβ oligomer formation can possibly lead to the development of more effective treatments for AD patients.