Vanderbilt Mass Spectrometry, Proteomics, and Lipidomics


VICB RESEARCH Mass Spectrometry, Proteomics, and Lipidomics
The past 20 years has seen an explosion in mass spectrometry technology, greatly facilitating the analysis of small molecules and macromolecules in a diverse range of contexts, including pure samples, complex mixtures, and even intact tissues. The Mass Spectrometry Research Center brings all of these new analytical modalities to Vanderbilt, and VICB investigators have not hesitated to capitalize on all of the advantages that state-of-the-art mass spectrometry has to offer. Dan Liebler applies the latest techniques of mass spectrometry-based proteomics to the analysis of complex protein mixtures in the search for new biomarkers of malignancy. A second goal of the lab is to characterize the protein damage caused by reactive electrophiles. Proteomics is also a focus in Andy Link’s work. He uses this approach to identify novel proteins and post-translational modifications associated with yeast ribosomes during the process of protein synthesis. Alex Brown uses mass spectrometry to analyze the complex array of lipids in cellular membranes in an effort to dissect precursor-product relationships in lipid signaling networks. His work represents a major contribution to the new discipline of lipidomics. Richard Caprioli’s ground-breaking work in the study of in vivo metabolism couples microdialysis sampling with mass spectrometric identification and quantification of key metabolites. This novel approach has allowed the Caprioli lab to track the metabolism of key neurotransmitters in the brain. His new approach to mass spectrometry-based imaging of proteins in intact tissue is discussed elsewhere (see Imaging). John McLean’s interest is in expanding the horizon for mass spectrometric analysis of complex biologic mixtures. His lab is exploring the application of two-dimensional gas-phase separations using ion mobility-mass spectrometry. This approach separates molecules on the basis of surface area in one dimension and mass-to-charge in the second dimension. Data are analyzed with the help of predictions made by molecular dynamics simulations. This method offers the advantage of separating molecules by major class (lipids versus peptides, versus carbohydrates, versus nucleotides) due to distinct surface area characteristics. Each class of molecule is then further separated on the basis of charge-to-mass ratio. This method offers great promise for biomarker discovery, metabolomics analysis, and detection of post-translational modifications and conformational changes in proteins. Dave Hachey is director of the Mass Spectrometry and Proteomics Core facilities of the Mass Spectrometry Research Center. In that position he collaborates with many other VICB members in the design and execution of mass spectrometry-based experiments and guarantees that the cores are current with the latest technology and methodology.
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The past 20 years has seen an explosion in mass spectrometry technology, greatly facilitating the analysis of small molecules and macromolecules in a diverse range of contexts, including pure samples, complex mixtures, and even intact tissues. The Mass Spectrometry Research Center brings all of these new analytical modalities to Vanderbilt, and VICB investigators have not hesitated to capitalize on all of the advantages that state-of-the-art mass spectrometry has to offer.

Dan Liebler applies the latest techniques of mass spectrometry-based proteomics to the analysis of complex protein mixtures in the search for new biomarkers of malignancy. A second goal of the lab is to characterize the protein damage caused by reactive electrophiles. Proteomics is also a focus in Andy Link’s work. He uses this approach to identify novel proteins and post-translational modifications associated with yeast ribosomes during the process of protein synthesis. Alex Brown uses mass spectrometry to analyze the complex array of lipids in cellular membranes in an effort to dissect precursor-product relationships in lipid signaling networks. His work represents a major contribution to the new discipline of lipidomics. Richard Caprioli’s ground-breaking work in the study of in vivo metabolism couples microdialysis sampling with mass spectrometric identification and quantification of key metabolites. This novel approach has allowed the Caprioli lab to track the metabolism of key neurotransmitters in the brain. His new approach to mass spectrometry-based imaging of proteins in intact tissue is discussed elsewhere (see Imaging).

John McLean’s interest is in expanding the horizon for mass spectrometric analysis of complex biologic mixtures. His lab is exploring the application of two-dimensional gas-phase separations using ion mobility-mass spectrometry. This approach separates molecules on the basis of surface area in one dimension and mass-to-charge in the second dimension. Data are analyzed with the help of predictions made by molecular dynamics simulations. This method offers the advantage of separating molecules by major class (lipids versus peptides, versus carbohydrates, versus nucleotides) due to distinct surface area characteristics. Each class of molecule is then further separated on the basis of charge-to-mass ratio. This method offers great promise for biomarker discovery, metabolomics analysis, and detection of post-translational modifications and conformational changes in proteins.

Dave Hachey is director of the Mass Spectrometry and Proteomics Core facilities of the Mass Spectrometry Research Center. In that position he collaborates with many other VICB members in the design and execution of mass spectrometry-based experiments and guarantees that the cores are current with the latest technology and methodology.