'Functional Amyloid and Biofilms: Lessons from Small Molecules and a Big Magnet'
Bacteria harbor dedicated machinery to assemble amyloid fibers at their cell surface to promote adhesion and biofilm formation. These dedicated assembly events are juxtaposed to the undesired protein mis-assembly events and formation of amyloid intermediates and amyloid fibers associated with eukaryotic diseases such as Alzheimer's disease.
Curli, produced by E. coli, are among the most well-studied bacterial amyloid. Moreover, bacterial pathogens form biofilms that have emerged as hallmarks of serious and persistent infectious diseases.
Cegelski's team is working to transform cartoon representations of the curli fiber into a molecular model using solid-state NMR spectroscopy. Her team has also discovered small molecules that influence curli assembly and biofilm formation and we are recruiting these as tools to probe biofilm structure and function using NMR and new biochemical assays.
Solid-state NMR can provide valuable information about intact biofilms and is uniquely suited to provide a quantitative perspective on biofilm composition, structure, and metabolism. In a broader context, our discoveries are helping to transform bacterial biofilm descriptors from vague terms like "glue" and "slime" to quantitative descriptions based on chemical composition and molecular architecture.
More information on her research can be found at http://www.stanford.edu/dept/chemistry/faculty/cegelski/.