With this award from the Major Research Instrumentation (MRI) program and the Chemistry Division, Kari B. Green-Church and colleagues David L. Denlinger, Joseph A. Krzycki, and Michael Ibba from Ohio State University and John Tansey from Otterbein College will acquire an ultra-high resolution time-of-flight mass spectrometer. The award will enhance research, research training and education at all levels. The mass spectrometer will support a variety of research projects including: (a) translational analysis of insect proteins during environmental stress and diapause; (b) mapping of the biosynthetic pathway of pyrrolysine and development of amino acid analogs; (c) the impact of MprF activity on lipid remodeling; (d) lipid profiling of apolipoprotein-like particles for studies of intracellular lipid trafficking.
Mass spectrometers (MS) are used to identify the chemical composition of a sample by measuring the mass of the molecular constituents in the sample after they are ionized and detected by the mass spectrometer. The time of flight (TOF) mass analyzer has high sensitivity and mass accuracy to assist the analyses and interpretation of the resultant data. The instrument will be configured and available as a cyberinstrument, meaning that access to and operation of the instrument is open to any academic institution in the Ohio Mass Spectrometry Consortium. The acquisition will provide graduate and undergraduate students training in this important technique at Ohio State University and other institutions in the state.
Mass spectrometry is an analytical tool that measures the masses of molecules and can provide structure information and quantitative data from simple to complex samples (biological, environmental and synthetic). This proposal to the Major Research Instrumentation Program (MRI) assisted the campus-wide Mass Spectrometry and Proteomics Facility (MS&P) at The Ohio State University in the purchase of a multi-user maXis™ Ultra-High resolution Time-of-Flight Mass Spectrometer (UHR-TOF MS) with collision induced dissociation (CID) and a Bruker AmaZon electron transfer dissociation (ETD) ion trap. The package also included software for proteomic and small molecule bioinformatic analyses. Since installation, the amaZon LCMS has analyzed 1513 LC-MS samples and 466 direct infusion samples. The maXis has analyzed 900 LC-MS samples and 251 direct infusion samples. The samples have been generated from 50 different research groups (PI’s) from the following colleges within OSU and outside institutions: Comprehensive Cancer Center, Pharmacy, Medicine, Engineering, Arts and Science, Food Agriculture and Environmental Science, Center of Emergent Materials, Education and Human Ecology, Dentistry, Dennison University, Youngstown State University, Miami University of Ohio, Ohio North University, Ashland University, Exciton Corp, Abitec, Lambent Corp, Quanta Biodesign and Invasc Theraputics. The instruments have also been used as self operated instruments providing excellent training opportunities for students and has been used for several formal lab classes for graduate and undergraduate students. Funding from NSF has greatly expanded the capabilities, services and educational outreach of the CCIC Mass Spectrometry and Proteomics Facility. Before our primary focus was proteomics and we now have expanded to lipidomics, metabolomics and other small molecule research areas (natural products, synthetic products etc). We also provide hands on training for high school, undergraduate and graduate level students. Access to high-end mass spectrometers allows and enriching education to students that makes them highly valuable in the the scientific community.
