The lab’s current research focus is on combining ultraviolet resonance Raman (UVRR) spectroscopy and chemometrics to study protein dynamics and peptide-small molecule interactions.

Phenomena associated with protein mis-folding are responsible for many disease related syndromes including Alzheimer’s disease. Proteins prone to mis-folding and aggregation are difficult to study by methods such as NMR due to their high degree of insolubility and the lack of persistent secondary structure. The ability to monitor short time scale events (ps-ms) makes vibrational spectroscopies (Resonance Raman, IR, etc…) more amenable to the study of these types of proteins, UVRR especially. Selective excitation of the polypeptide backbone amide by UV light reduces the number of non-structurally sensitive Raman bands in the UVRR spectra of proteins.

Multidimensional resonance Raman (MDRR) spectra, such as this simulated two-dimensional Raman excitation-scattering spectrum represents a unique type of data that may be exploited to aide in the a priori deconvolution of the highly overlapped Raman bands of proteins. Current research projects involve developing robust chemometric methods for analysis of these multidimensional UVRR spectra for modeling peptide secondary structure, folding and conformational transitions.

Several small molecules have been identified that reduce the toxicity, inhibit aggregation or reverse aggregation of the β-amyloid (Aβ) peptide involved in Alzheimer’s disease. These molecules vary greatly in structure and their mode of action is unknown or under question in some cases. Our lab is interested in using UVRR to correlate these molecules’s effectiveness at inhibiting Aβ aggregation with their mode of action, enabling the development of a rapid screening method for potential Aβ aggregation inhibitors.