In addition our group is highly collaborative and we routinely generate substrate specificity profiles of endo- and exo-peptidases that have been isolated from diverse organisms that includes ticks, crustaceans and parasitic worms.

My laboratory interests lie in the detection and characterization of proteolytic enzymes that are involved in disease. In particular, we are interested in understanding the role of peptidases/proteases at host-pathogen and tumor-stroma interfaces. Our research utilizes a mass spectrometry based platform technology to uncover the global proteolytic activity in complex biological samples such as the secretions of cancer cells and infectious organisms.

Our workflow also includes in-depth proteomic analysis to identify the enzymes. Knowledge of which peptidases are functionally active in diseased tissue and not active in healthy tissue allow us to 1) develop peptidase inhibitors to shut down the function, 2) generate peptidase-activated imaging agents to locate the disease or 3) develop peptidase-activated drugs to aid in the delivery of toxic compounds to the site of disease. Using this technology, we have uncovered novel proteolytic activities in gastric juice, pancreatic cyst fluid, serum and neutrophil extracts.