Distinguished Research Professor Biography Jon Amster earned his B.A. in Chemistry from Cornell University in 1977 and his Ph.D. in Analytical Chemistry in 1986, also from Cornell. After postdoctoral research at the University of California at Irvine, he joined the faculty of the University of Georgia in 1988 as an Assistant Professor of Chemistry, where he now holds the title of Distinguished Research Professor. He served as Head of Chemistry from 2009-2019, and Interim Head from 2022-2023. His research interests are in high performance mass spectrometry and its applications to bioanalytical chemistry. Education Education: Ph.D. Cornell University, 1986 M.S. Cornell University, 1983 B.A. Cornell University, 1977 Research Research Areas: Analytical Chemistry Biological Chemistry Research Interests: My research group specializes in the development and application of Fourier transform mass spectrometry for solving difficult problems in bioanalytical chemistry. We are exploring new methods for analyzing the structural features of glycosaminoglycans (GAGs), a class of carbohydrates that play a central role in a number of important biological processes, including cellular communication, cell signaling, and regulation of biochemical pathways. Our approach uses electron-aided methods of ion activation (electron detachment dissociation, electron induced dissociation, and electron transfer dissociation) to dissociate GAG oligosaccharides, and to provide detailed data regarding sites of sulfation, acetylation, and uronic acid stereochemistry. We are exploring the use of chemometric analysis (principal component analysis and partial least squares discriminant analysis) for maximizing the amount of analytical information that can be extracted from the highly complex tandem mass spectra produced by electron detachment dissociation of GAGs. We are developing rapid and sensitive methods for measuring changes in the cellular levels of proteins. Our approach is to harvest complex protein mixtures from a cell, enzymatically digest the proteins into peptides, and to identify the peptides by accurate mass measurement using Fourier transform mass spectrometry. This process is aided by a combination of capillary scale separation methods, chemical derivitization methods using compounds synthesized in our laboratory, and isotope labeling. Other recent research projects include the use of advanced computational methods for carrying out multiparticle simulations of ion motion within the FTICR mass analyzer. These simulations give detailed information about ion-ion interactions, and provide insight into the limits of mass accuracy in FTICR mass spectrometry. Selected Publications Selected Publications: 2023-2024 Davis, A. R.; Roberts, E. T.; Amster, I. J.; Barb, A. W. “Uniform [13C,15N]-Labeled and Glycosylated IgG1 Fc Expressed in Saccharomyces cerevisiae”, J. Biomol. NMR 2024, 78, 9-18. DOI: 10.1007/s10858-023-00428-1 Subedi, G. P.; Roberts E. T.; Davis, A. R.; Kremer, P. G.; Amster, I. J.; Barb, A. W. “A Comprehensive Assessment of Selective Amino Acid 15N-Labeling in Human Embryonic Kidney 293 Cells for NMR Spectroscopy”, J. Biomol. NMR2024, published online. DOI: 10.1007/s10858-023-00434-3 Lin, P.-H.; Xu, Y.; Bali, S. K.; Kim, J.; Gimeno, A.; Roberts, E. T.; James, D.; Almeida, N. S.; Loganathan, N.; Wilson, A.; Amster, I. J.; Moremen, K.; Liu, J.; Jiménez-Barbero, J.; Huang, X. “Expedient Solid Phase Supported Chemo-Enzymatic Synthesis of Chondroitin Sulfate Proteoglycan Glycopeptides”, Angew. Chemie. 2024, 63, e202405671. DOI: 10.1002/anie.202405671 Roberts, E. T.; Davis, A. R.; Risher, J. T.; Barb, A. W.; Amster, I. J. “Automated Assignment of 15N And 13C Enrichment Levels in Doubly-Labeled Proteins”, J. Am. Soc. Mass Spectrom. 2024, 35, 2344-2357. DOI: 10.1021/jasms.4c00218 Glenn, C. K.; El Hajj, O.; McQueen, Z.; Poland, R.; Penland, R.; Roberts, E.; Choi, J.; Bai, B.; Shin, N.; Anosike, A.; Kumar, K.; Abdurrahman, M.; Liu, P.; Amster, I. J.; Smith, G.; Flanagan, S.; Callaham, M; Loudermilk, E.; O’Brien, J.; Saleh, R. “Brown Carbon Emissions for Biomass Burning Under Wildfire and Prescribed-Fire Conditions”, ACS EST Air 2024, 1, 1124-1136. DOI: 10.1021/acsestair.4c00089 Maciej-Hulme, M; van Gemst, J. J.; Sanderson, P.; Rops, A. L. W. W. M. M.; Berden, J. H.; Smeets, B.; Amster, I. J.; van der Vlag, J. “Glomerular Endothelial Glycocalyx-Derived Heparan Sulfate Inhibits Glomerular Leukocyte Influx and Attenuates Experimental Glomerulonephritis”, Front. Mol. Biosci. 2023, 10, 1177560. DOI: 10.3389/fmolb.2023.1177560 2021-2022 Williams, R. V.; Huang, C.; McDermott, C.; Columbus, L.; Moremen, K. W.; Prestegard, J. H.; Amster, I. J. “Site-to-Site Crosstalk in OSTB Glycosylation of hCEACAM1-IgV”, Proc. Natl. Acad. Sci. USA 2022, 119, e2202992119. DOI: 10.1073/pnas.2202992119 Williams, R. V.; Huang, C.; Moremen, K. W.; Amster, I. J.; Prestegard, J. H. “NMR Analysis Suggests the Terminal Domains of Robo1 Remain Extended but are Rigidified in the Presence of Heparan Sulfate”, Sci. Rep. 2022, 12, 14769. DOI: 10.1038/s41598-022-18769-6 Shaver, A. O.; Garcia, B. M.; Gouveia, G. J.; Morse, A. M.; Liu, Z.; Asef, C. K.; Borges, R. M.; Leach III, F. E.; Andersen, E. C.; Amster, I.J.; Fernández, F. M.; Edison, A. S.; McIntyre, L. M. “An Anchored Experimental Design and Meta-Analysis Approach to Address Batch Effects in Large-Scale Metabolomics”, Front. Mol. Biosci. 2022, 9, 930204. DOI: 10.3389/fmolb.2022.930204 Lampros, E. A.; Kremer, P. G.; Aquilar Diaz de Leon, J. S.; Roberts, E. T.; Amster, I. J.; Barb, A. W. “The Antibody-Binding Fc Gamma Receptor IIIa / CD16a is N-Glycosylated with High Occupancy at All Five Sites”, Curr. Res. Immunol. 2022, 3, 128-135. DOI: 10.1016/j.crimmu.2022.05.005 Konermann, L.; Amster, I. J.; Smith, J. C.; Verhaert, P. D. E. M. “The 33rd International Tandem Mass Spectrometry Workshop, Lake Louise, Alberta, Canada”, J. Am. Soc. Mass Spectrom. 2022, 33, 409-411. DOI: 10.1021/jasms.2c00028 Pepi, L. E.; Amster, I. J. “Electron-Activated Tandem Mass Spectrometry Analysis of Glycosaminoglycans”, Curr. Protoc. 2021, 1, e83. DOI: 10.1002/cpz1.83 Rogals, M. J.; Yang, J. Y.; Williams, R. V.; Moremen, K. W.; Amster, I. J.; Prestegard, J. H. “Sparse Isotope Labeling for NMR of Glycoproteins Using 13C-Glucose”, Glycobiology 2021, 31, 425-435. DOI: 10.1093/glycob/cwaa071 Pepi, L. E.; Sanderson, P.; Stickney, M.; Amster, I. J. “Developments in Mass Spectrometry for Glycosaminoglycan Analysis: A Review”, Mol. Cell. Proteomics 2021, 20, 100025. DOI: 10.1074/mcp.r120.002267 Pepi, L. E.; Leach III, F. E.; Klein, D. R.; Brodbelt, J. S.; Amster, I. J. “Investigation of the Experimental Parameters of Ultraviolet Photodissociation for the Structural Characterization of Chondroitin Sulfate Glycosaminoglycan Isomers”, J. Am. Soc. Mass Spectrom. 2021, 32, 1759-1770. DOI: 10.1021/jasms.1c00119 Huang, D.; Bouza, M. A.; Gaul, D. A.; Leach, F. E.; Amster, I. J.; Schroeder, F.; Edison, A. S.; Fernández, F. M. “Comparison of High-Resolution Fourier Transform Mass Spectrometry Platforms for C. Elegans Metabolite Annotation Purposes”, Anal. Chem. 2021, 93, 12374-12382. DOI: 10.1021/acs.analchem.1c02224 Spliid, C. B.; Toledo, A. G.; Sanderson, P.; Mao, Y.; Gatto, F.; Gustavsson, T.; Choudhary, S.; Vogelsang, R. P.; Gögenur, I.; Theander, T. G.; Leach, F. E.; Amster, I. J. Esko, J. D.; Clausen, T. M. “The Specificity of the Malarial VAR2CSA Protein for Chondroitin Sulfate Depends on 4-O-Sulfation and Accessibility to the Ligand”, J. Biol. Chem. 2021, 297, 101391. DOI: 10.1016/j.jbc.2021.101391 2019-2020 Driver, J. A.; Kharchenko, A.; Amster, I. J. “Simulations of Nw Measurement Using Multiple Detection Electrodes in FTICR Mass Spectrometry”, Int. J. Mass Spectrom. 2020, 455, 116372. DOI: 10.1016/j.ijms.2020.116372 Yu, Y.; Zhang, F.; Amster, I. J.; Renois-Predalus, G.; Linhardt, R. J. “Filter-Entrapment Enrichment Pull-Down Assay for Glycosaminoglycan Structural Characterization and Protein Interaction”, Carbohydr. Polym. 2020, 245, 116623. DOI: 10.1016/j.carbpol.2020.116623 Pepi, L. E.; Sasiene, Z. J.; Mendis, P.; Jackson, G. P.; Amster, I. J. “Structural Characterization of Sulfated Glycosaminoglycans Using Charge Transfer Dissociation”, J. Am. Soc. Mass Spectrom. 2020, 31, 2143-3153. DOI: 10.1021/jasms.0c00252 Han, X.; Sanderson, P.; Nesheiwat, S.; Lin, L.; Yu, Y.; Zhang, F.; Amster, I. J.; Linhardt, R. J. “Structural Analysis of Urinary Glycosaminoglycans from Healthy Human Subjects”, Glycobiology 2020, 30, 143-151. DOI: 10.1093/glycob/cwz088 Duan, J.; Amster, I. J. “A Scoring Algorithm for the Automated Analysis of Glycosaminoglycan MS/MS Data”, J. Am. Soc. Mass Spectrom. 2019, 30, 2692-2703. DOI: 10.1007/s13361-019-02338-9 Stickney, M.; Sanderson, P.; Leach III, F. E.; Zhang, F.; Linhardt, R. J.; Amster, I. J. “Online Capillary Zone Electrophoresis Negative Electron Transfer Dissociation Tandem Mass Spectrometry of Glycosaminoglycan Mixtures”, Int. J. Mass Spectrom. 2019, 445, 116209. DOI: 10.1016/j.ijms.2019.116209 Stickney, M.; Xia, Q.; Amster, I. J. “Investigation of Electrospray for a Capillary Electrophoresis-Mass Spectrometry Interface in Reverse Polarity and Negative Ion Mode”, Eur. J. Mass Spectrom. 2019, 25, 157-163. DOI: 10.1177/1469066719828192 Klein, D. R.; Leach, F. E. III; Amster, I. J.; Brodbelt, J. S. “Structural Characterization of Glycosaminoglycans Using 193 nm Ultraviolet Photodissociation”, Anal. Chem. 2019, 91, 6019-6026. DOI: 10.1021/acs.analchem.9b00521 Williams, R. V.; Yang, J.-Y.; Moremen, K. W.; Amster, I. J.; Prestegard, J. H. “Measurement of Residual Dipolar Couplings in Methyl Groups via Carbon Detection”, J. Biomolec. NMR 2019, 73, 191-198. DOI: 10.1007/s10858-019-00245-5 2017-2018 Sanderson, P.; Stickney, M.; Leach, F. E., III; Xia, J.; Yu, Y.; Zhang, F.; Linhardt, R. J.; Amster, I. J. “Heparin/Heparan Sulfate Analysis by Capillary Zone Electrophoresis-Mass Spectrometry”, J. Chromatogr. A 2018, 1545, 75-83. DOI: 10.1016/j.chroma.2018.02.052. Aebersold, R.; Agar, J. N.; Amster, I. J.; Baker, M.; Bertozzi, C. R.; Costello, C. E.; Cravatt, B. J.; Fenselau, C.; Garcia, B.; Ge, Y.; Gunawardena, J.; Hendrickson, R. C.; Hergenrother, P. J.; Huber, C.; Ivanov, A. R.; Jensen, O.; Jewett, M. C.; Kelleher, N. L.; Kiessling, L. L.; Krogan, N. J.; Larsen, M. R.; Loo, J. A.; Loo, R. R.; Lundberg, E.; MacCoss, M.; Mallick, P.; Mootha, V. K.; Muir, T. W.; Patrie, S. M.; Pesavento, J. J.; Pitteri, S. J.; Rodriguez; H.; Sandoval, W.; Schluter, H.; Sheeley, D. M.; Slavoff, S. A.; Smith, L. M.; Snyder, M. P.; Thomas, P. M.; Uhlen, M.; van der Donk, W. A.; van Eyk, J. E.; Vidal, M.; Walt, D. R.; White, F. M.; Williams, E. R.; Wohlschlager, T.; Wysocki, V. H.; Yates, N. A.; Young, N. L. “How Many Human Proteoforms are There?”, Nat. Chem. Biol. 2018, 14, 206-214. DOI: 10.1038/nchembio.2576. Driver, J. A.; Nagornov, K. O.; Kozhinov, A. N.; Tsybin, Y. O.; Kharchenko, A.; Amster, I. J., “Multiparticle Simulations of Quadrupolar Ion Detection in an Ion Cyclotron Resonance Cell with Narrow Aperture Detection Electrodes”, J. Am. Soc. Mass Spectrom. 2018, 29, 51-62. DOI: 10.1007/s13361-017-1817-6. Agyekum, I.; Pepi, L.; Yu, Y.; Li, J.; Yan, L.; Linhardt, R. J.; Chen, S.; Amster, I. J., “Structural Elucidation of Fucosylated Chondroitin Sulfates from Sea Cucumber Using FTICR-MS/MS”, Eur. J. Mass Spectrom. 2018, 24, 157-167. DOI: 10.1177/1469066717731900. Yu, Y.; Duan, J.; Leach, F. E., III; Toida, T.; Zhang, H.; Zhang, F.; Amster, I. J.; Linhardt, R. J. “Sequencing the Dermatan Sulfate Chain of Porcine Decorin”, J. Am. Soc. Chem. 2017, 139, 16986-16995. DOI: 10.1021/jacs.7b10164. Leach, F. E., III; Riley, N. M.; Westphall, M. S.; Coon, J. J.; Amster, I. J., “Negative Electron Transfer Dissociation Sequencing of Increasingly Sulfated Glycosaminoglycan Oligosaccharides on an Orbitrap Mass Spectrometer”, J. Am. Soc. Mass Spectrom. 2017, 28, 1844-1854. DOI: 10.1007/s13361-017-1709-9. Agyekum, I; Zong, C.; Boons, G.-J.; Amster, I. J., “Single Stage MS/MS Analysis of the C-5 Uronic Acid Stereochemistry in Heparan Sulfate Tetrasaccharides Using Electron Detachment Dissociation”, J. Am. Soc. Mass Spectrom. 2017, 28, 1741-1750. DOI: 10.1007/s13361-017-1643-x. Chen, Y.; Lin, L.; Agyekum, I.; Zhang, X.; St. Ange, K.; Yu, Y.; Liu, J.; Amster, I. J.; Linhardt, R. J., “Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants”, J. Pharm. Sci. 2017, 106, 973-981. DOI: 10.1016/j.xphs.2016.11.023. Lin, L.; Liu, X.; Zhang, F.; Chi, L.; Amster, I. J.; Leach III, F. E.; Xia, Q.; Linhardt, R. J. “Analysis of Heparin Oligosaccharides by Capillary Electrophoresis-Negative-Ion Electrospray Ionization Mass Spectrometry”, Analyt. Bioanalyt. Chem. 2017, 409, 411-420. DOI: 10.1007/s00216-016-9662-1. Zhao, Y.; Singh, A.; Xu, Y.; Zong, C.; Zhang, F.; Boons, G.-J.; Liu, J.; Linhardt, R. L; Woods, R. J.; Amster, I. J., “Gas-Phase Analysis of the Complex of Fibroblast Growth Factor 1 with Heparan Sulfate: A Traveling Wave Ion Mobility Spectrometry (TWIMS) and Molecular Modeling Study”, J. Am. Soc. Mass Spectrom. 2017, 28, 96-109. DOI: 10.1007/s13361-016-1496-8.
