Welcome to the Thanh Do research group home page! The lab is actively seeking motivated students in the areas of biophysical and bioanalytical chemistry. No mass spectrometry background is required. Interested undergraduate and graduate students are invited to contact Professor Do via email about joining the lab. My research combines ion-mobility mass spectrometry (IM-MS), mass spectrometry imaging (MSI), and computational modeling to bring a chemical physics outlook to problems of broad chemical interest. The overarching aims of my research are twofold. The first is to develop fast and sensitive MS-based techniques and bioanalytical methods suitable for simultaneously assessing the structure, topology, composition and dynamics of exotic species in the gas phase. These species include small molecules, peptides and proteins in complex mixtures and volume-limited samples. Specifically, my research group will couple state-of-the-art MS technologies and computational modeling to explore previously uncharacterized, transient and metastable species by performing fragmentation or spectroscopy on mass-to-charge and drift mobility-selected ions. I will also take advantage of weakly solvent-bound complexes and protomers which are sensitive to structural change and charge location, respectively, to enhance the separation capability of IM-MS. The work is a blend of experiment and theory. The second overarching aim is to use these techniques for biological applications. A focal area is to investigate toxic mechanisms induced by amyloid oligomers through probing changes in chemical content of single cells or neurons of transgenic animals and human biopsies. Amyloid oligomers have been implicated as toxic agents in debilitating diseases such as Alzheimer’s, type 2 diabetes and amyotrophic lateral sclerosis. High-throughput single cell profiling provides a unique approach to elucidate the toxic mechanisms of amyloid oligomers in a native-like condition, and to identify the potential therapeutic treatments for devastating diseases. Other applications involve study of bacterial α-helix fibrils, and the un-threading and re-threading processes of lasso peptides, their conformational switch and thermal stability, as well as their ability to act as conformation trap for other peptides.