Associate Professor Lynette Cegelski's research is inspired by the challenge and importance of elucidating chemical structure and function in biological systems and the need for new and unconventional approaches to solve outstanding problems in biology and medicine. Lynette completed her undergraduate studies in Chemistry at SUNY-Binghamton, New York (B.S. summa cum laude and Phi Beta Kappa 1998), where she participated in research to determine the microtubule-bound conformation of the anti-cancer drug Taxol by REDOR solid-state NMR. This formative experience motivated her move to Washington University to conduct her PhD training in the laboratory of Professor Jacob Schaefer, where she trained as a solid-state NMR spectroscopist (Ph.D. Chemistry 2004). She investigated bacterial and plant cell-wall and whole-cell systems. She examined the mode of action of vancomycin and oritavancin and also examined photosynthesis and photorespiration in intact leaf NMR experiments. She trained in Microbiology and Infectious Disease research as a postdoctoral fellow in Molecular Microbiology at the Washington University School of Medicine, working with Professor Scott Hultgren. There, she introduced the first small-molecule inhibitors of functional amyloid assembly in bacteria. She joined the faculty of the Stanford Chemistry Department in 2008. The Cegelski Research program integrates chemistry, biology, and physics to investigate the assembly and function of macromolecular and whole-cell systems. They are revealing new bacterial structures, uncovering fundamental parameters of chemical composition and architecture in complex biofilm assemblies, and identifying new anti-infective strategies. Cegelski's work has garnered early career awards, including the Burroughs Wellcome Career Award at the Scientific Interface, the 2010 NIH Director’s New Innovator Award, the National Science Foundation CAREER Award, and the Presidential Early Career Award for Scientists and Engineers (PECASE).
Romaniuk, J. A. H., & Cegelski, L. (2015). Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 370(1679).
Cegelski, L. (2015). Bottom-up and top-down solid-state NMR approaches for bacterial biofilm matrix composition. Journal of Magnetic Resonance , 253, 91–97.
Maher, M. C., Lim, J. Y., Gunawan, C., & Cegelski, L. (2015). Cell-Based High-Throughput Screening Identifies Rifapentine as an Inhibitor of Amyloid and Biofilm Formation in Escherichia coli. ACS INFECTIOUS DISEASES, 1(10), 460–468.
Reichhardt, C., Jacobson, A. N., Maher, M. C., Uang, J., McCrate, O. A., Eckart, M., & Cegelski, L. (2015). Congo Red Interactions with Curli-Producing E. coli and Native Curli Amyloid Fibers. PloS One, 10(10).
McCrate, O. A., Zhou, X., & Cegelski, L. (2013). Curcumin as an amyloid-indicator dye in E. coli. Chemical Communications , 49(39), 4193–95.
Lim, J. Y., May, J. M., & Cegelski, L. (2012). Dimethyl Sulfoxide and Ethanol Elicit Increased Amyloid Biogenesis and Amyloid-Integrated Biofilm Formation in Escherichia coli. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 78(9), 3369–78.
Thongsomboon, W., Werby, S. H., & Cegelski, L. (2020). Evaluation of Phosphoethanolamine Cellulose Production among Bacterial Communities using Congo Red Fluorescence. Journal of Bacteriology.
Neville, L. F., Shalit, I., Warn, P. A., Scheetz, M. H., Sun, J., Chosy, M. B., … Rendell, J. T. (2021). In vivo targeting of E. coli with vancomycin-arginine. Antimicrobial Agents and Chemotherapy.
Reichhardt, C., McCrate, O. A., Zhou, X., Lee, J., Thongsonboom, W., & Cegelski, L. (2016). Influence of the amyloid dye Congo red on curli, cellulose, and the extracellular matrix in E. coli during growth and matrix purification. Influence of the Amyloid Dye Congo Red on Curli, Cellulose, and the Extracellular Matrix in E. Coli during Growth and Matrix Purification, 408(27).
Acheson, J. F., Ho, R., Goularte, N. F., Cegelski, L., & Zimmer, J. (2021). Molecular organization of the E. coli cellulose synthase macrocomplex. Nature Structural & Molecular Biology, 28(3), 310–18.