The Orsburn Lab

Research

We specialize in the analysis of atypical biomolecules by mass spectrometry. Work here ranges from the analysis of post-translationally modified proteins through products of drug metabolism, with many stops in between.
Modern mass spectrometry requires collaborative interfaces with clinicians and biologists, method development at the bench and the instrument and new informatics.

Applying single cell proteomics to understand resistance to chemotherapies

Cancer recurrence can begin with a single cell that has survived a chemotherapy regimen. 
We specialize in the application of single cell proteomics (SCP) by mass spectrometry to better understand the response of individual cells to drugs. 
We first study the phenotypic responses of cells treated with drugs with proteomics of thousands of homogenized cells. Once responses are identified, we use single cell proteomics to understand the level of heterogeneity that exists in this response at a cellular level.

Leveraging scalable computing to obtain unprecedented coverage of the human proteome

LCMS based proteomics typically relies on desktop computing architecture. While these workflows allow us to identify most human protein groups, they do not allow us to understand the actual proteoforms of interest. By leveraging scalable Cloud based platforms we can study proteomics in a true biological context. Using this approach we can identify human mutations without the need for expensive genomics input.  Our recent work has identified hundreds of cell surface neo-antigens on the surface of cancer cells and resulted in the most comprehensive proteome of human tumors ever assembled.

Modernizing clinical assays with mass spectrometry

Many assays used for patient diagnostics have not changed in any meaningful way in decades. We have identified both metabolic and proteomic assays of low sensitivity or specificity. We were recently awarded our first collaborative grant to replace a historic neonatal assay requiring multiple blood draws with something better, faster, and less invasive for children.

Want to collaborate?

725 N. Wolfe Street Baltimore, MD
Biophysics 304/B11-B11A
Physiology 312

b-orsburn-1-@jhmi.edu (remove the dashes)