The Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases

Center for Proteomics and Systems Biology

David Gorenstein, Ph.D., Professor, Director and Deputy Director

Chuantao, Jiang, Ph.D., Assistant Professor

Kevin Rosenblatt, M.D., Ph.D., Associate Professor

David Volk, Ph.D., Assistant Professor

The Centers for Proteomics and Systems Biology connect research efforts across the university in systems biology, clinical and translational sciences, protein chemistry, genomics, and proteomics, bringing together people to promote intellectual exchange and the the transfer of expertise in these key fields and beyond.

Multi-Departmental Collaboration of Interacting Centers

The IMM is the hub of a new alliance connecting research efforts across the university in systems biology, clinical and translational sciences, protein chemistry, genomics, and proteomics. This new multidisciplinary science will link the efforts of various centers, bringing together people to promote intellectual exchange and the transfer of expertise in these key fields and beyond.

Proteomics is emerging as an exciting, new area of science. While genomics has been highly successful at cataloging nucleic acid sequences, for the vast majority of genes it is the protein products that are functional. Further, proteins are the targets for essentially all of the drugs on the market today. Gene sequences give us a starting point, but most cellular proteins are extensively processed and modified. To understand cellular regulation, elucidate disease processes, and
identify drug targets we need the detailed characterization of proteins that now appears achievable through mass spectrometry.

One mission of the Center for Proteomics and Systems Biology (CPSB) will be to develop the experimental and analytical technologies that will make this a reality. One important area of development for the CPSB will be the identification of biomarkers for disease, including prevention and treatment. The CPSB will not only develop new
technologies but provide a coordinated group of centers and programs for collaborative and service work to the UTH community in cutting edge proteomics, protein chemistry and systems biology research. The IMM is an ideal environment for bringing together resources and leadership in the experimental and computational programs.
The main Mass Spectroscopy Facility is located in the IMM and houses a Voyager STR MALDI mass spectrometer, an Agilent 1100 LC/MSD Trap, an Applied Biosystems QStar Elite Q-ToF tandem LCMSMS and a Thermo LTQ Orbitrap equipped with an Eksigent LC system. The facility has 1D and 2D HPLC systems to provide high resolution separation
of peptides and proteins for in depth proteomic analysis of cells, tissues or biological fluids. The entire facility is supported by the CCTS Genologics LIMS system which is used for de-identified sample tracking from the bedside to analytical results from genomic, proteomic and immunological characterization. This instrumentation group is a state of the art mass spectroscopy core that is capable of providing routine mass spectroscopy services such as protein identification and peptide profiling, more demanding analyses such as post-translational  modifications, and quantitative peptide and protein analyses in complex mixtures.

Hubs of Research Collaboration

  • Protein Chemistry examines the structural analysis of proteins while addressing a range of diseases including neurodegenerative diseases.
  • Proteomics seeks to understand cellular regulation, elucidate disease processes, and identify drug targets using the detailed characterization of proteins achievable through mass spectrometry.
  • Systems Biology we are developing a first class, high visibility research program on proteogenomics, the synthesis of genomics an and proteomics, using advanced algorithms for signal processing, data analysis and information handling.
  • Proteomics Core Laboratory of the Center for Clinical and Translational Sciences provides proteomics analysis services such as protein identification, analysis of differential expression and post-translational modifications of protein, as well as analysis and interpretation of results.