Mary L. Kraft
Assistant Professor of Chemical & Biomolecular Engineering
Affliliate, Department of Chemistry
Professor Mary L. Kraft received her BS degree in 1998 from the University of Illinois at Chicago, and her PhD degree in Chemistry from the University of Illinois at Urbana-Champaign in 2003. After working as a postdoctoral fellow at Stanford University, she joined the faculty of the Department of Chemical and Biomolecular Engineering in 2007. Dr. Kraft has also served as an affiliate professor in the Department of Chemistry since that time.
Imaging Mass Spectrometry of Biomaterials
Our ability to engineer tissues and biomimetic devices hinges upon an understanding of the structure-function relationship in healthy and diseased cells. Our laboratory utilizes materials characterization, quantitative engineering principles, cell biology and chemistry to elucidate the influence of molecular organization on cellular function.
Imaging Mass Spectrometry for Glycosylation
Glycosylated cell membrane components modulate cell adhesion, migration, differentiation, and recognition. Changes in the glycosylation patterns displayed on the cell membrane are hallmarks of many diseases, including cancer. Some abnormal glycan structures have been linked to specific diseases, but the full range of structural changes and the functional roles of the glycans remain undiscovered.
Imaging secondary ion mass spectrometry (SIMS) is a direct approach to image the chemical composition at the sample surface with sub-micron lateral resolution. We are developing an imaging mass spectrometry-based approach to analyze the glycan composition in cell membranes. This strategy to identify and image membrane glycan structures that are associated with specific phenotypes can lead to a better understanding of their functional significance in disease progression.
Composition Analysis of the Influenza Virus Pre-Envelope Domain
The site of influenza virus assembly in the host cell, which is called the influenza virus pre-envelope domain, is hypothesized to be enriched with cholesterol and sphingolipids. To evaluate this hypothesis, the lipid composition at the small region of the cell membrane that is abundant in viral envelope proteins must be determined. We are developing a multiple isotope imaging mass spectrometry-based approach to analyze the membrane composition at the site of virus budding. These studies can substantially increase our understanding of influenza virus pathogenesis.
Moore, J. S. and Kraft, M. L. Synchronized self-assembly, Science 2008, 320, 620-621.
M. L. Kraft, P. K. Weber, M. L. Longo, I. D. Hutcheon, and S. G. Boxer, "Phase separation of lipid membranes analyzed with high-resolution secondary ion mass spectrometry , " Science, 313, 1948-1951 (2006).
M. L. Kraft, S. F. Fishel, C. Galli Marxer, P. K. Weber, I. D. Hutcheon, and S. G. Boxer, "Quantitative analysis of supported membrane composition using the NanoSIMS," Applied Surface Science, 252, 6950-6956 (2006).
- Burroughs Welcome Career Award at the Scientific Interface
- Kirschstein Postdoctoral Fellow; National Institutes of Health (NIH)
Cover article of Biophysical Journal
C. Galli Marxer, M. L. Kraft, P. K. Weber, I. D. Hutcheon, and S. G. Boxer, "Supported membrane composition analysis by secondary ion mass spectrometry with high lateral resolution , " Biophysical Journal, 88, 2965-2975 (2005).