About This Webinar
2D IR spectroscopy is a powerful tool for understanding how protein structure changes and the dynamics of that process. The combination of 2D IR and 13C18O isotope labeling has previously been used in literature to better understand the aggregation pathway of amyloid proteins and identify intermediate species that precede fibril formation. Amyloid proteins are characterized by their formation of extended ß-sheet structures, or fibrils, and are associated with diseases such as type II diabetes and Alzheimer’s disease.
In addition to the fibrils, soluble intermediates or oligomers are also known to be cytotoxic thus there is an interest in understanding what types of materials impact the formation and lifetime of such species. Previous research has identified that nanoparticles (NPs) can impact the aggregation process, but identification of intermediate species has proven difficult. This problem has lead to interest in using 2D IR spectroscopy to identify those species and understand changes to the aggregation mechanism.
As NPs become increasingly prevalent in nanomedicine as well as other industries, it is important to understand how they interact with different amyloid proteins. Hess highlights using 2D IR and isotope labeling, where it was shown that gold NPs inhibit the aggregation of human islet amyloid polypeptide and preliminary results suggest that gold NPs prolong the lifetime of a previously identified oligomer species.
*** This presentation premiered during the
2023 BioPhotonics Conference. For more information on Photonics Media conferences and summits, visit
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About the presenter
Kayla Hess is a doctoral candidate in Lauren Buchanan, Ph.D.’s lab at Vanderbilt University. She received a bachelor’s degree in chemistry from Elizabethtown College in 2018 and began her doctoral studies at Vanderbilt in 2018, where she has been using two-dimensional infrared spectroscopy to study amyloid aggregation dynamics and protein-nanoparticle interactions.