Home Department: undeclared
Mentor: Danielle Mai (Chemical Engineering)

“Protease-Activated Elastin-Like Polypeptides with GFP”

Inducing a slower, more stable diffusion of medicine and targeted drug delivery, an issue in modern medicine administration today, could be enabled through enzymatically altering a soluble drug protein locally and changing it from soluble to solid. This is the motivation behind Jesse’s summer project. Previous research has been conducted on proteases excising hydrophilic portions (soluble) of an elastin-like protein (ELP) and subsequently coagulating (turning solid). Jesse’s project would expand upon this by investigating the phenomenon in the context of an ELP attached to a protein with more complex folded tertiary structure, GFP, rather than the simple unfolded ELP alone.