Determination of cleavage site specificity of matrix metalloproteases by assay of a peptide library generated by enzymatic digest of a complete or partial proteome

Mass spectrometry is a technique for separating and identifying molecules based on mass. It’s an important tool in proteomic investigations, the analysis of the whole set of proteins expressed in a cell. Recent advances in mass spectrometry have enabled the identification of thousands of unknown nd uncharacterized proteins. Many of these proteins are proteases, enzymes responsible for splitting specific peptide bonds (primary links of protein structures). Patrick Beaudette is studying a protease family known as matrix metalloproteases (MMPs). MMPs regulate a variety of cell processes, from the degradation of structural proteins to the activation and inactivation of cell signaling pathways. Proteins proteolytically processed under these circumstances can have implications in a variety of disease symptoms, ranging from inflammation to tumor growth. Beaudette’s research focuses on identifying the substrates (molecules upon which enzymes act) that a particular MMP protein splits, and the mechanism by which it locates these substrates within the cell. The research may lead to a fuller understanding of the function of the MMP family of enzyes and the role it plays within a cell. The findings could contribute to the design of inhibitors for MMPs for use in therapy of cancer and other conditions.