Modern Spectroscopy Lab

FTIR (Fourier-transform infrared spectroscopy) is a useful tool for collecting structural and chemical information about proteins. We are very interested in structural changes that potential drugs can cause in Amyloid-β (AB) folding and aggregation. 

 

AB is a small protein consisting of 36 to 43 amino acids, and is the primary component of amyloid plaques found in Alzheimer’s patients. The accumulation of AB in the brain is necessary in the progression of Alzheimer’s disease. Measuring how  the peptide accumulates, aggregates, and is degraded by proteases under different conditions is central to understanding and treating this ailment.  Because of the nature of this protein, monitoring how it behaves can be a technical challenge. The aggregation of AB is in a constant flux between different aggregation states. This makes it difficult to measure the state of the aggregates at an exact time point. FTIR offers a unique opportunity to overcome the limitations inherent in other (slower) assays as it allows the precise characterization of the aggregates in a matter of seconds. These advantages help overcome the reproducibility problems that usually coincide with other methods (1,2), and help us verify the findings obtained using other assays.
 

1. Faller, P., & Hureau, C. (2021). Reproducibility problems of amyloid-β self-assembly and how to deal with them. Frontiers in Chemistry, 8. https://doi.org/10.3389/fchem.2020.611227

2. Foley, A. R., & Raskatov, J. A. (2020). Assessing Reproducibility in Amyloid β Research: Impact of Aβ Sources on Experimental Outcomes. ChemBioChem, 21(17), 2425–2430. https://doi.org/10.1002/cbic.202000125