Jeffrey Spraggins (Presenter)
Vanderbilt University
Bio: Jeffrey M. Spraggins received his B.A. in Chemistry from the College of Wooster and his Ph.D. in Analytical Chemistry from the University of Delaware (2009), where he studied gas-phase fragmentation mechanisms of modified biomolecules and metal-sulfide cluster ion-molecule reactions. Dr. Spraggins continued his training as a postdoctoral research fellow in Richard Caprioli’s research group and is currently a Research Assistant Professor in the Departments of Chemistry and Biochemistry and a member of the Mass Spectrometry Research Center at Vanderbilt University. His research focuses on developing new mass spectrometric technologies to enhance biomolecular imaging experiments. Specifically, he is working on expanding the application of FTICR MS for the spatial analysis and structural identification of metabolites, lipids, peptides and proteins in biological tissues.
Authorship: Jeffrey M. Spraggins (1), Raf Van de Plas (2), Jessica L. Moore (1), David G. Rizzo (1), and Richard Caprioli (1)
(1) Vanderbilt University, Nashville, TN (2) Delft University of Technology, Delft, Netherlands
| Short Abstract MALDI imaging mass spectrometry is a highly sensitive and selective tool used to visualize biomolecules in tissue. However, imaging of proteins remains a difficult task relative to lipids and metabolites. High-resolution protein imaging experiments have been limited by both sensitivity and throughput. Identification strategies have been restricted by insufficient mass accuracy to confidently link IMS to proteomics data. Here, we demonstrate next-generation imaging capabilities using MALDI-IMS. FTICR IMS provides unprecedented mass resolving power and accuracy for proteins up to ~18kDa, enabling identification based on correlation with LC-MS/MS proteomics data. High-speed MALDI-TOF platforms enable protein images to be collected at rates >20 px/s, facilitating new applications that require large number of pixels. |
Long Abstract
MALDI imaging mass spectrometry is a highly sensitive and selective tool used to visualize biomolecules in tissue. However, imaging of proteins remains a difficult task relative to lipids and metabolites. High-resolution protein imaging experiments have been limited by both sensitivity and throughput. Identification strategies have been restricted by insufficient mass accuracy to confidently link IMS to proteomics data. Here, we demonstrate next-generation imaging capabilities using MALDI-IMS. FTICR IMS provides unprecedented mass resolving power and accuracy for proteins up to ~18kDa, enabling identification based on correlation with LC-MS/MS proteomics data. High-speed MALDI-TOF platforms enable protein images to be collected at rates >20 px/s, facilitating new applications that require large number of pixels.
References & Acknowledgements:
The authors wish to acknowledge the support of grants from the NIH/NIGMS (5 P41 GM103391-04 and 5R01 GM058008) and the National Institutes of Health Shared Instrumentation Grant Program (1S10OD012359-01) awarded to RMC and the National Institute of Allergy and Infectious Diseases (R01 AI101171-01A1 and R21 AI107233) awarded to Eric Skaar in support of JLM. DGR is supported by the Aegis Sciences Fellowship in Chemistry, Vanderbilt University. JLM is supported by Vanderbilt Chemical Biology Interface training program (T32 GM 065086) and the Mitchum Warren Graduate Research Fellowship.
| Description | Y/N | Source |
| Grants | yes | NIH |
| Salary | no | |
| Board Member | no | |
| Stock | no | |
| Expenses | no |
IP Royalty: no
| Planning to mention or discuss specific products or technology of the company(ies) listed above: | no |