Aubrey received a B.A. from Macalester College, where she majored in Chemistry with a minor in Biology. While at Macalester she worked with Prof. Ronald Brisbois on ’desilylative click’ methodology. After graduating from Macalester in 2012, Aubrey interned at Eli Lilly in research and development. Fall 2012, Aubrey began her PhD research in the University Wisconsin Madison’s Chemistry doctoral program. At UW, Aubrey joined the Raines research group, where she studies collagen mimetic peptides for wound healing and understanding bacterial infection.
Collagen is the most abundant protein in humans and comprises a major structural component of the extracellular matrix (ECM). In wounds, collagen triple helices suffer damage. As collagen prefers to form a triple helix, we can take advantage of the damaged collagen and introduce collagen mimetic peptides (CMPs) that will adhere to the wound surface. These invasive strand CMPs can thereby deliver a payload to the collagen surface of a wound. Nature may also use this invasive strand mechanism as a form of host infection. Invasion of host tissue can be mediated by the interaction of bacterial surface proteins and the ECM. Group A Streptococcus (GAS) displays cell-surface proteins that resemble human collagen. We hypothesize that the collagen-like strands of GAS form triple helices with denatured collagen in a wound bed. The ensuing adherence could be a basis for infection by GAS. To test this hypothesis, we are using fluorophore-labeled CMPs to detect collagen strands on the surface of live GAS cells. We are also evaluating a knock-in expression of collagen-like strands, Scl 1 and Scl 2, on the surface of B. subtilis for transferring the ability to anneal to our CMPs. With these tools we hope to understand and ultimately antagonize infections by GAS.