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I-Corps: Enhanced Protein Discovery Tools for Proteomics Research

$50,000FY2016TIPNSF

Carnegie Mellon University, Pittsburgh PA

Investigators

Abstract

The broader impact/commercial potential of this I-Corps project focuses on developing tools for the biomedical research community, in particular the discovery of proteins that are altered during the normal or abnormal functioning of cells, tissues and organisms. The term for this protein discovery field is proteomics. Hundreds of thousands of proteomics samples are analyzed around the world annually. These innovations will significantly benefit the biomedical research community. These tools will allow scientists to understand complex processes such as how the microbiome affects behavior, how development is affected by genetic mutations, and how cancer cells change their behavior upon chemotherapy. The number of questions these tools can help address is limitless. All major research institutions have proteomics facilities that serve dozens to hundreds of researchers. These tools will be used both by individual research labs and proteomics core facilities, as well as contract research facilities and pharma companies. This I-Corps project addresses technological needs in the field of proteomics. A very large fraction of proteomics samples involve separating complex mixtures of different proteins into individual protein species by a process called gel electrophoresis, where electric currents are used to separate proteins by size and charge in thin slabs of gel material. This work concentrates on two key unmet needs. First is improving the detection sensitivity of proteins within electrophoresis gels. Convention detection instruments can detect proteins over a 1,000-fold concentration range, but proteins normally exist in cells over a million-fold range. The device developed here is capable of detecting proteins over a million-fold concentration range. The next unmet need is to efficiently transfer proteins from gels to a mass spectrometer, which is used to chemically characterize proteins. The method under development here will greatly increase the throughput of this process.

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