Jessica Prenni
Joint Faculty, Assistant Professor, Director Of Proteomic & Metabolomics FacilityOffice: Microbiology C121Phone: 970-491-0961Education: Ph.D., University of ColoradoEmail: Jessica.Prenni@Colostate.eduResearch Title: Mass Spectrometry Based Proteomics and Metabolomics
Proteomics and Metabolomics are fields of scientific study which combine techniques in purification and separation, mass spectrometry and bioinformatics. In our lab we utilize these tools for the identification and characterization of proteins and small molecules in a variety of biological systems.
Our lab focuses on the use and application of analytical techniques such as liquid chromatography, 2-dimensional gel electrophoresis, and mass spectrometry for the analysis and characterization of proteins and small molecules.
Proteomics: The proteome is most commonly defined as the entire complement of proteins expressed in a given cell type or tissue under a given condition. A proteomics experiment involves the digestion of a protein or mixture of proteins into peptides using an enzyme such as trypsin and the analysis of these peptides by mass spectrometry. In a mass spectrometer we can measure the mass of the peptides as well as the masses of fragment ions formed during the analysis. Using bioinformatic tools we can use the resulting lists of experiment peptide masses and fragment ion masses to indentify the protein(s). These measured masses can also be used to identify and map sites of post translational modification or to monitor changes in protein expression under varying conditions.
Metabolomics: Our primary focus is on discovery based metabolic profiling of biological fluids. Small molecule metabolites can be extracted from all means of biological fluids (plasma, serum, urine, etc.) to plant extracts and secreted fluids. Separation of metabolites is performed using ultra performance liquid chromatography (UPLC), and the mass of each metabolite is measured using a quadrupole time-of-flight mass spectrometer (Q-TOF). For each component in each sample (e.g. serum from control vs diseased animals) a mass, intensity, and retention time is recorded and using multivariate statistical analysis we can identify molecules that are contributing to the separation of sample groups. We can then further investigate these components, or potential biomarkers, by molecular formula prediction based on mass and fragmentation of the molecules with comparison to that of standard compounds.
Selected Publications
Bhamidi, S.; Scherman, M.S.; Rithner, C.D.; Prenni, J.E.; Chatterjee, D.; Khoo, K.; and McNeil, M.R. The Identification and Location of Succinyl Residues and the Characterization of the Interior Arabinan Region Allows for a Model of the Complete Primary Structure of Mycobacterium Tuberculosis Mycolyl Arabinogalactan Journal of Biological Chemistry, 2008, 283(19), 12992-13000.
Dooley, G.P.; Reardon, K.F.; Prenni, J.E.; Legare, M.E.; Foradori, C.D.; Tessari, J.E.; and Hanneman, W.H. Proteomic Analysis of Diaminochlorotriazine (DACT) Adducts in Wister Rat Pituitary Glands and LbetaT2 Rat Pituitary Cells Chemical Research in Toxicology, 2008, 21(4), 844-851.
Prenni, J.E.; Swardson-Olver, C.J. Proteomics: A Review and an Illustration Veterinary Clinical Pathology, 2007, 36(1) 13-24.
Dooley, G.P.; Prenni, J.E.; Cranmer, B.K.; Prentiss P.L.; Andersen, M.E.; Tessari, J.D. Identification of a Novel Hemoglobin Adduct in Sprague Dawley Rats Exposed to Atrazine Chemical Research In Toxicology, 2006, 19(5), 692-700.
Prenni, J.E.; Shen, Z.; Trauger, S.; Chen, W.; Siuzdak, G. Protein Characterization using Liquid Chromatography Desorption/Ionization on Silicon Mass Spectrometry (LC-DIOS-MS) Spectroscopy, 2003, 17, 693-698.
Go, E.P.; Prenni, J.E.; Wei, J.; Jones, A.; Hall, S.C.; Witkowska, H.E.; Shen, Z.; Siuzdak, G. Desporption/Ionization on Silicon Time-of-Flight/Time-of-Flight Mass Spectrometry Analytical Chemistry, 2003, 75, 2504-2506.