Dr. Lammi and her students use molecular spectroscopy – in bulk solution and at the level of single particles – to investigate research questions of interest. Current studies focus on (A) folding, oligomerization, and aggregation inhibition in Alzheimer’s amyloid-b peptide (Ab) and (B) fluorescence spectroscopy of ZnO nanoparticles.
A. Folding, Oligomerization, and Aggregation Inhibition in Alzheimer’s Amyloid-b Peptide
Amyloid-b (Ab) is a peptide of 39-43 amino acids that is created by the enzymatic cleavage of the amyloid precursor protein (APP). It readily self-assembles into a diverse array of oligomers and aggregates which are thought to be causative agents in Alzheimer’s disease. Our group has utilized single-particle fluorescence spectroscopy to monitor oligomerization, one peptide species at a time, and to probe structures and conformational change in individual Ab dimers. We are currently collaborating with Dr. Hanna’s group in the design, synthesis, and evaluation of small-molecule inhibitors of Ab aggregation.
B. Fluorescence Spectroscopy of ZnO Nanoparticles
Zinc oxide is a II-VI semiconductor with a direct band gap of 3.37 eV (375 nm). Its high electron mobility and strong luminescence make it favorable for use in light-emitting diodes (LEDs), among other applications. Nanoparticles of ZnO are among the most commonly produced nanomaterials, used extensively in sunscreen (where they absorb UV light); ZnO nanoparticles (NPs) are also being widely studied for their antimicrobial properties. Dr. Gelabert’s lab is synthesizing ZnO NPs by hydrothermal methods; we are collaborating on their spectroscopic characterization, via steady-state and time-resolved bulk fluorescence and single-particle methods.