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Journal articles on the topic 'High-throughput mass spectrometry'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Want, Elizabeth, Michael Greig, Bruce Compton, Ben Bolaños, and Gary Siuzdak. "Mass spectrometry in high throughput analysis." Spectroscopy 17, no. 4 (2003): 663–80. http://dx.doi.org/10.1155/2003/949412.

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2

Shen, Luhou, Johnny Zhang, Qian Yang, Nicholas E. Manicke, and Zheng Ouyang. "High throughput paper spray mass spectrometry analysis." Clinica Chimica Acta 420 (May 2013): 28–33. http://dx.doi.org/10.1016/j.cca.2012.10.025.

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3

Han, Jun, Raju Datla, Sammy Chan, and Christoph H. Borchers. "Mass spectrometry-based technologies for high-throughput metabolomics." Bioanalysis 1, no. 9 (December 2009): 1665–84. http://dx.doi.org/10.4155/bio.09.158.

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4

Zhang, Hui, Chang Liu, Wenyi Hua, Lucien P. Ghislain, Jianhua Liu, Lisa Aschenbrenner, Stephen Noell, et al. "Acoustic Ejection Mass Spectrometry for High-Throughput Analysis." Analytical Chemistry 93, no. 31 (July 28, 2021): 10850–61. http://dx.doi.org/10.1021/acs.analchem.1c01137.

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5

Chalk, Rod, Georgina Berridge, Leela Shrestha, Claire Strain-Damerell, Pravin Mahajan, Wyatt Yue, Opher Gileadi, and Nicola Burgess-Brown. "High-Throughput Mass Spectrometry Applied to Structural Genomics." Chromatography 1, no. 4 (October 9, 2014): 159–75. http://dx.doi.org/10.3390/chromatography1040159.

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6

Maurer, Hans H., and Frank T. Peters. "Toward High-Throughput Drug Screening Using Mass Spectrometry." Therapeutic Drug Monitoring 27, no. 6 (December 2005): 686–88. http://dx.doi.org/10.1097/01.ftd.0000180224.19384.f0.

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7

Bakhtiar, R., and F. L. S. Tse. "High-throughput chiral liquid chromatography/tandem mass spectrometry." Rapid Communications in Mass Spectrometry 14, no. 13 (2000): 1128–35. http://dx.doi.org/10.1002/1097-0231(20000715)14:13<1128::aid-rcm1>3.0.co;2-5.

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8

Forbes, Chris D., Joshuaine G. Toth, Can C. Özbal, William A. Lamarr, Jennifer A. Pendleton, Sandra Rocks, Richard W. Gedrich, David G. Osterman, James A. Landro, and Kevin J. Lumb. "High-Throughput Mass Spectrometry Screening for Inhibitors of Phosphatidylserine Decarboxylase." Journal of Biomolecular Screening 12, no. 5 (August 2007): 628–34. http://dx.doi.org/10.1177/1087057107301320.

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A high-throughput mass spectrometry assay to measure the catalytic activity of phosphatidylserine decarboxylase (PISD) is described. PISD converts phosphatidylserine to phosphatidylethanolamine during lipid synthesis. Traditional methods of measuring PISD activity are low throughput and unsuitable for the high-throughput screening of large compound libraries. The high-throughput mass spectrometry assay directly measures phosphatidylserine and phosphatidylethanolamine using the RapidFire™ platform at a rate of 1 sample every 7.5 s. The assay is robust, with an average Z′ value of 0.79 from a screen of 9920 compounds. Of 60 compounds selected for confirmation, 54 are active in dose-response studies. The application of high-throughput mass spectrometry permitted a high-quality screen to be performed for an otherwise intractable target. ( Journal of Biomolecular Screening 2007:628-634)

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9

Cupp-Sutton, Kellye A., and Si Wu. "High-throughput quantitative top-down proteomics." Molecular Omics 16, no. 2 (2020): 91–99. http://dx.doi.org/10.1039/c9mo00154a.

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10

Clendinen, Chaevien S., María Eugenia Monge, and Facundo M. Fernández. "Ambient mass spectrometry in metabolomics." Analyst 142, no. 17 (2017): 3101–17. http://dx.doi.org/10.1039/c7an00700k.

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11

Menzel, Christoph, Vincent Guillou, Markus Kellmann, Valery Khamenya, Michael Juergens, and Peter Schulz-Knappe. "High-Throughput Biomarker Discovery and Identification by Mass Spectrometry." Combinatorial Chemistry & High Throughput Screening 8, no. 8 (December 1, 2005): 743–55. http://dx.doi.org/10.2174/138620705774962373.

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12

Guthals, Adrian, Jeramie D. Watrous, Pieter C. Dorrestein, and Nuno Bandeira. "The spectral networks paradigm in high throughput mass spectrometry." Molecular BioSystems 8, no. 10 (2012): 2535. http://dx.doi.org/10.1039/c2mb25085c.

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13

Janiszewski, J. S., M. C. Swyden, and H. G. Fouda. "High-Throughput Method Development Approaches for Bioanalytical Mass Spectrometry." Journal of Chromatographic Science 38, no. 6 (June 1, 2000): 255–58. http://dx.doi.org/10.1093/chromsci/38.6.255.

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14

McDonnell, Liam A., Alexandra van Remoortere, René J. M. van Zeijl, Hans Dalebout, Marco R. Bladergroen, and André M. Deelder. "Automated imaging MS: Toward high throughput imaging mass spectrometry." Journal of Proteomics 73, no. 6 (April 2010): 1279–82. http://dx.doi.org/10.1016/j.jprot.2009.10.011.

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15

Chamrad, Daniel C., Gerhard Koerting, Johan Gobom, Herbert Thiele, Joachim Klose, Helmut E. Meyer, and Martin Blueggel. "Interpretation of mass spectrometry data for high-throughput proteomics." Analytical and Bioanalytical Chemistry 376, no. 7 (August 1, 2003): 1014–22. http://dx.doi.org/10.1007/s00216-003-1995-x.

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16

Li, Li-Ping, Bao-Sheng Feng, Jian-Wang Yang, Cui-Lan Chang, Yu Bai, and Hu-Wei Liu. "Applications of ambient mass spectrometry in high-throughput screening." Analyst 138, no. 11 (2013): 3097. http://dx.doi.org/10.1039/c3an00119a.

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17

Colinge, Jacques, Alexandre Masselot, Marc Giron, Thierry Dessingy, and Jérôme Magnin. "OLAV: Towards high-throughput tandem mass spectrometry data identification." PROTEOMICS 3, no. 8 (August 2003): 1454–63. http://dx.doi.org/10.1002/pmic.200300485.

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18

Zhu, Haijing, and Guangming Huang. "High-throughput paper spray mass spectrometry via induced voltage." Rapid Communications in Mass Spectrometry 33, no. 4 (January 30, 2019): 392–98. http://dx.doi.org/10.1002/rcm.8336.

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19

Pereira, Luisa, Paul Ross, and Mark Woodruff. "Chromatographic aspects in high throughput liquid chromatography/mass spectrometry." Rapid Communications in Mass Spectrometry 14, no. 5 (March 15, 2000): 357–60. http://dx.doi.org/10.1002/(sici)1097-0231(20000315)14:5<357::aid-rcm889>3.0.co;2-b.

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20

Moini, Mehdi, Longfei Jiang, and Samir Bootwala. "High-throughput analysis using gated multi-inlet mass spectrometry." Rapid Communications in Mass Spectrometry 25, no. 6 (February 15, 2011): 789–94. http://dx.doi.org/10.1002/rcm.4924.

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21

Wu, Xiang, Jing Wang, Lory Tan, John Bui, Erik Gjerstad, Kirk McMillan, and Wentao Zhang. "In Vitro ADME Profiling Using High-Throughput RapidFire Mass Spectrometry." Journal of Biomolecular Screening 17, no. 6 (March 29, 2012): 761–72. http://dx.doi.org/10.1177/1087057112441013.

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Early assessment of absorption, distribution, metabolism, and excretion (ADME) properties of drug candidates has become an essential component of modern drug discovery. ADME characterization is important in identifying compounds early that are likely to fail in later clinical development because of suboptimal pharmacokinetic properties or undesirable drug-drug interactions. Proper utilization of ADME results, meanwhile, can prioritize candidates that are more likely to have good pharmacokinetic properties and also minimize potential drug-drug interactions. By integrating a RapidFire system with an API4000 mass spectrometer (RF-MS), we have established a high-throughput capability to profile compounds (>100 compounds/wk) in a panel of ADME assays in parallel with biochemical and cellular characterizations. Cytochrome P450 inhibition and time-dependent inhibition assays and microsomal stability assays were developed and fully optimized on the system. Compared with the classic liquid chromatography–mass spectrometry method, the RF-MS system generates consistent data with approximately 20-fold increase in throughput. The lack of chromatographic separation of compounds, substrates, and metabolites can complicate data interpretation, but this occurs in a small number of cases that are readily identifiable. Overall, this system has enabled a real-time and quantitative measurement of a large number of ADME samples, providing a rapid evaluation of clinically important drug-drug interaction potential and drug metabolic stability.

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22

Guerrera, Ida Chiara, and Oliver Kleiner. "Application of Mass Spectrometry in Proteomics." Bioscience Reports 25, no. 1-2 (February 4, 2005): 71–93. http://dx.doi.org/10.1007/s10540-005-2849-x.

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Mass spectrometry has arguably become the core technology in proteomics. The application of mass spectrometry based techniques for the qualitative and quantitative analysis of global proteome samples derived from complex mixtures has had a big impact in the understanding of cellular function. Here, we give a brief introduction to principles of mass spectrometry and instrumentation currently used in proteomics experiments. In addition, recent developments in the application of mass spectrometry in proteomics are summarised. Strategies allowing high-throughput identification of proteins from highly complex mixtures include accurate mass measurement of peptides derived from total proteome digests and multidimensional peptide separations coupled with mass spectrometry. Mass spectrometric analysis of intact proteins permits the characterisation of protein isoforms. Recent developments in stable isotope labelling techniques and chemical tagging allow the mass spectrometry based differential display and quantitation of proteins, and newly established affinity procedures enable the targeted characterisation of post-translationally modified proteins. Finally, advances in mass spectrometric imaging allow the gathering of specific information on the local molecular composition, relative abundance and spatial distribution of peptides and proteins in thin tissue sections.

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23

McLaren, David G., Vinit Shah, Thomas Wisniewski, Lucien Ghislain, Chang Liu, Hui Zhang, and S. Adrian Saldanha. "High-Throughput Mass Spectrometry for Hit Identification: Current Landscape and Future Perspectives." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 2 (January 22, 2021): 168–91. http://dx.doi.org/10.1177/2472555220980696.

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For nearly two decades mass spectrometry has been used as a label-free, direct-detection method for both functional and affinity-based screening of a wide range of therapeutically relevant target classes. Here, we present an overview of several established and emerging mass spectrometry platforms and summarize the unique strengths and performance characteristics of each as they apply to high-throughput screening. Multiple examples from the recent literature are highlighted in order to illustrate the power of each individual technique, with special emphasis given to cases where the use of mass spectrometry was found to be differentiating when compared with other detection formats. Indeed, as many of these examples will demonstrate, the inherent strengths of mass spectrometry—sensitivity, specificity, wide dynamic range, and amenability to complex matrices—can be leveraged to enhance the discriminating power and physiological relevance of assays included in screening cascades. It is our hope that this review will serve as a useful guide to readers of all backgrounds and experience levels on the applicability and benefits of mass spectrometry in the search for hits, leads, and, ultimately, drugs.

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24

Wilson, Dean, Xiaoli Wang, Erin Walsh, and Robyn Rourick. "High Throughput Log D Determination Using Liquid Chromatography-Mass Spectrometry." Combinatorial Chemistry & High Throughput Screening 4, no. 6 (September 1, 2001): 511–19. http://dx.doi.org/10.2174/1386207013330913.

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25

TAKEMORI, Nobuaki. "High-Throughput Quantitative Analysis of Transmembrane Proteins using Mass Spectrometry." Seibutsu Butsuri 56, no. 2 (2016): 116–19. http://dx.doi.org/10.2142/biophys.56.116.

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26

Yates, John R., Edwin Carmack, Lara Hays, and Jimmy Eng. "High Throughput Analysis of Tandem Mass Spectrometry Data for Peptides." Laboratory Automation News 2, no. 2 (May 1997): 28–31. http://dx.doi.org/10.1177/221106829700200206.

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In recent years tandem mass spectrometry has made a substantial impact on the sequence analysis of peptides ( 1 ). In this process peptide ions are dissociated in a collision cell to produce a collection of fragment ions. The m/z values of the fragment ions are determined in the second mass analyzer. Fortuitously, peptide ions fragment primarily around the amide linkages or peptide bonds in a manner that produces a ladder of sequence ions. This method of analysis for peptides has several advantages; high throughput and sensitivity, the ability to analyze peptides contained in mixtures, and lastly the ability to observe covalent modifications to the structure.

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27

Wleklinski, Michael, Bradley P. Loren, Christina R. Ferreira, Zinia Jaman, Larisa Avramova, Tiago J. P. Sobreira, David H. Thompson, and R. Graham Cooks. "High throughput reaction screening using desorption electrospray ionization mass spectrometry." Chemical Science 9, no. 6 (2018): 1647–53. http://dx.doi.org/10.1039/c7sc04606e.

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28

Monforte, Joseph A., and Christopher H. Becker. "High-throughput DNA analysis by time-of-flight mass spectrometry." Nature Medicine 3, no. 3 (March 1997): 360–62. http://dx.doi.org/10.1038/nm0397-360.

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29

Pluchinsky, Adam J., Daniel J. Wackelin, Xiongyi Huang, Frances H. Arnold, and Milan Mrksich. "High Throughput Screening with SAMDI Mass Spectrometry for Directed Evolution." Journal of the American Chemical Society 142, no. 47 (November 11, 2020): 19804–8. http://dx.doi.org/10.1021/jacs.0c07828.

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30

Purvine, Samuel, Natali Kolker, and Eugene Kolker. "Spectral Quality Assessment for High-Throughput Tandem Mass Spectrometry Proteomics." OMICS: A Journal of Integrative Biology 8, no. 3 (September 2004): 255–65. http://dx.doi.org/10.1089/omi.2004.8.255.

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31

Erhard, Florian, and Ralf Zimmer. "Detecting outlier peptides in quantitative high-throughput mass spectrometry data." Journal of Proteomics 75, no. 11 (June 2012): 3230–39. http://dx.doi.org/10.1016/j.jprot.2012.03.032.

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32

Kim, Yun-Gon, Yung-Hun Yang, and Byung-Gee Kim. "High-throughput characterization of lipopolysaccharide-binding proteins using mass spectrometry." Journal of Chromatography B 878, no. 31 (December 1, 2010): 3323–26. http://dx.doi.org/10.1016/j.jchromb.2010.10.001.

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33

Hofstadler, Steven A., Thomas A. Hall, Kristin A. Sannes-Lowery, Sheri Manalili, Jessica E. Paulsen, Leslie D. McCurdy, Lora Gioeni, et al. "Analysis of DNA forensic markers using high throughput mass spectrometry." Forensic Science International: Genetics Supplement Series 2, no. 1 (December 2009): 524–26. http://dx.doi.org/10.1016/j.fsigss.2009.08.140.

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34

Manicke, Nicholas E., Thomas Kistler, Demian R. Ifa, R. Graham Cooks, and Zheng Ouyang. "High-throughput quantitative analysis by desorption electrospray ionization mass spectrometry." Journal of the American Society for Mass Spectrometry 20, no. 2 (February 2009): 321–25. http://dx.doi.org/10.1016/j.jasms.2008.10.011.

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35

Uchiyama, Noriko, Douglas R. Dougan, J. David Lawson, Hitomi Kimura, Shin-ichi Matsumoto, Yukiya Tanaka, and Tomohiro Kawamoto. "Identification of AHCY inhibitors using novel high-throughput mass spectrometry." Biochemical and Biophysical Research Communications 491, no. 1 (September 2017): 1–7. http://dx.doi.org/10.1016/j.bbrc.2017.05.107.

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36

de Rond, Tristan, Megan Danielewicz, and Trent Northen. "High throughput screening of enzyme activity with mass spectrometry imaging." Current Opinion in Biotechnology 31 (February 2015): 1–9. http://dx.doi.org/10.1016/j.copbio.2014.07.008.

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37

Palmblad, Magnus, Yuri E. M. Burgt, Ekaterina Mostovenko, Hans Dalebout, and André M. Deelder. "A novel mass spectrometry cluster for high-throughput quantitative proteomics." Journal of the American Society for Mass Spectrometry 21, no. 6 (June 2010): 1002–11. http://dx.doi.org/10.1016/j.jasms.2010.02.001.

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38

Gao, Xia, Kevin Bain, Jeffery B. Bonanno, Michelle Buchanan, Davin Henderson, Don Lorimer, Curtis Marsh, et al. "High-throughput Limited Proteolysis/Mass Spectrometry for Protein Domain Elucidation." Journal of Structural and Functional Genomics 6, no. 2-3 (September 2005): 129–34. http://dx.doi.org/10.1007/s10969-005-1918-5.

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39

Schneider, Bradley B., D. J. Douglas, and David D. Y. Chen. "Multiple sprayer system for high-throughput electrospray ionization mass spectrometry." Rapid Communications in Mass Spectrometry 16, no. 20 (2002): 1982–90. http://dx.doi.org/10.1002/rcm.806.

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40

Kyranos, James N., Hong Cai, Darren Wei, and Wolfgang K. Goetzinger. "High-throughput high-performance liquid chromatography/mass spectrometry for modern drug discovery." Current Opinion in Biotechnology 12, no. 1 (February 2001): 105–11. http://dx.doi.org/10.1016/s0958-1669(00)00176-2.

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41

Lee, Young Jin, Rachael C. Leverence, Erica A. Smith, Justin S. Valenstein, Kapil Kandel, and Brian G. Trewyn. "High-Throughput Analysis of Algal Crude Oils Using High Resolution Mass Spectrometry." Lipids 48, no. 3 (January 19, 2013): 297–305. http://dx.doi.org/10.1007/s11745-013-3757-7.

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42

Anderson, Sarah E., Natalie S. Fahey, Jungsoo Park, Patrick T. O'Kane, Chad A. Mirkin, and Milan Mrksich. "A high-throughput SAMDI-mass spectrometry assay for isocitrate dehydrogenase 1." Analyst 145, no. 11 (2020): 3899–908. http://dx.doi.org/10.1039/d0an00174k.

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43

Bandaru, Pradeep, Mukesh Bansal, and Ilya Nemenman. "Mass Conservation and Inference of Metabolic Networks from High-Throughput Mass Spectrometry Data." Journal of Computational Biology 18, no. 2 (February 2011): 147–54. http://dx.doi.org/10.1089/cmb.2010.0222.

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44

Masselon, Christophe, Gordon A. Anderson, Richard Harkewicz, James E. Bruce, Ljiljana Pasa-Tolic, and Richard D. Smith. "Accurate Mass Multiplexed Tandem Mass Spectrometry for High-Throughput Polypeptide Identification from Mixtures." Analytical Chemistry 72, no. 8 (April 2000): 1918–24. http://dx.doi.org/10.1021/ac991133+.

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45

Beckmann, Manfred, David Parker, David P. Enot, Emilie Duval, and John Draper. "High-throughput, nontargeted metabolite fingerprinting using nominal mass flow injection electrospray mass spectrometry." Nature Protocols 3, no. 3 (February 28, 2008): 486–504. http://dx.doi.org/10.1038/nprot.2007.500.

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46

Liebisch, Gerhard, Wolfgang Drobnik, Bernd Lieser, and Gerd Schmitz. "High-Throughput Quantification of Lysophosphatidylcholine by Electrospray Ionization Tandem Mass Spectrometry." Clinical Chemistry 48, no. 12 (December 1, 2002): 2217–24. http://dx.doi.org/10.1093/clinchem/48.12.2217.

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Abstract Background: Lysophosphatidylcholine (LPC) has been suggested to play a functional role in various diseases, including atherosclerosis, diabetes, and cancer mediated by LPC-specific G-protein-coupled receptors. Initial studies provided evidence for a potential use of LPC as diagnostic maker. However, existing methodologies are of limited value for a systematic evaluation of LPC species concentrations because of complicated, time-consuming procedures. We describe a methodology based on electrospray ionization tandem mass spectrometry (ESI-MS/MS) applicable for high-throughput LPC quantification. Methods: Crude lipid extracts of EDTA-plasma samples were used for direct flow injection analysis. LPC 13:0 and LPC 19:0 were added as internal standards, and the ESI-MS/MS was operated in the parent-scan mode for m/z 184. Quantification was achieved by standard addition. Data processing was highly automated by use of the mass spectrometer software and self-programmed Excel macros. Results: The calibrators LPC 16:0, LPC 18:0, and LPC 22:0 showed a linear response independent of sample dilution and plasma cholesterol concentration for both internal standards. The within-run imprecision (CV) was 3% for the major and 12% for the minor species, whereas the total imprecision was ∼12% for the major and 25% for the minor species. The detection limit was <1 μmol/L. Conclusion: The developed ESI-MS/MS methodology with an analysis time of 2 min/sample, simple sample preparation, and automated data analysis allows high-throughput quantification of distinct LPC species from plasma samples, which could be a valuable tool for the evaluation of LPC as diagnostic marker.

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47

Roberts, M. L., J. R. Burton, K. L. Elder, B. E. Longworth, C. P. McIntyre, K. F. von Reden, B. X. Han, et al. "A High-Performance 14C Accelerator Mass Spectrometry System." Radiocarbon 52, no. 2 (2010): 228–35. http://dx.doi.org/10.1017/s0033822200045252.

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A new and unique radiocarbon accelerator mass spectrometry (AMS) facility has been constructed at the Woods Hole Oceanographic Institution. The defining characteristic of the new system is its large-gap optical elements that provide a larger-than-standard beam acceptance. Such a system is ideally suited for high-throughput, high-precision measurements of 14C. Details and performance of the new system are presented.

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48

Rankin, Naomi J., Karl Burgess, Stefan Weidt, Goya Wannamethee, Naveed Sattar, and Paul Welsh. "High-throughput quantification of carboxymethyl lysine in serum and plasma using high-resolution accurate mass Orbitrap mass spectrometry." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 56, no. 3 (March 4, 2019): 397–407. http://dx.doi.org/10.1177/0004563219830432.

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Background Carboxymethyl lysine is an advanced glycation end product of interest as a potential biomarker of cardiovascular and other diseases. Available methods involve ELISA, with potential interference, or isotope dilution mass spectrometry (IDMS), with low-throughput sample preparation. Methods A high-throughput sample preparation method based on 96-well plates was developed. Protein-bound carboxymethyl lysine and lysine were quantified by IDMS using reversed phase chromatography coupled to a high-resolution accurate mass Orbitrap Exactive mass spectrometer. The carboxymethyl lysine concentration (normalized to lysine concentration) was measured in 1714 plasma samples from the British Regional Heart Study (BRHS). Results For carboxymethyl lysine, the lower limit of quantification (LLOQ) was estimated at 0.16 μM and the assay was linear between 0.25 and 10 μM. For lysine, the LLOQ was estimated at 3.79 mM, and the assay was linear between 2.5 and 100 mM. The intra-assay coefficient of variation was 17.2% for carboxymethyl lysine, 9.3% for lysine and 10.5% for normalized carboxymethyl lysine. The inter-assay coefficient of variation was 18.1% for carboxymethyl lysine, 14.8 for lysine and 16.2% for normalized carboxymethyl lysine. The median and inter-quartile range of all study samples in each batch were monitored. A mean carboxymethyl lysine concentration of 2.7 μM (IQR 2.0–3.2 μM, range 0.2–17.4 μM) and a mean normalized carboxymethyl lysine concentration of 69 μM/M lysine (IQR 54–76 μM/M, range 19–453 μM/M) were measured in the BRHS. Conclusion This high-throughput sample preparation method makes it possible to analyse large cohorts required to determine the potential of carboxymethyl lysine as a biomarker.

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49

Castro, Daniel C., Yuxuan Richard Xie, Stanislav S. Rubakhin, Elena V. Romanova, and Jonathan V. Sweedler. "Image-guided MALDI mass spectrometry for high-throughput single-organelle characterization." Nature Methods 18, no. 10 (September 30, 2021): 1233–38. http://dx.doi.org/10.1038/s41592-021-01277-2.

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AbstractPeptidergic dense-core vesicles are involved in packaging and releasing neuropeptides and peptide hormones—critical processes underlying brain, endocrine and exocrine function. Yet, the heterogeneity within these organelles, even for morphologically defined vesicle types, is not well characterized because of their small volumes. We present image-guided, high-throughput mass spectrometry-based protocols to chemically profile large populations of both dense-core vesicles and lucent vesicles for their lipid and peptide contents, allowing observation of the chemical heterogeneity within and between these two vesicle populations. The proteolytic processing products of four prohormones are observed within the dense-core vesicles, and the mass spectral features corresponding to the specific peptide products suggest three distinct dense-core vesicle populations. Notable differences in the lipid mass range are observed between the dense-core and lucent vesicles. These single-organelle mass spectrometry approaches are adaptable to characterize a range of subcellular structures.

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50

Lowe, Denise M., Michelle Gee, Carl Haslam, Bill Leavens, Erica Christodoulou, Paul Hissey, Philip Hardwicke, et al. "Lead Discovery for Human Kynurenine 3-Monooxygenase by High-Throughput RapidFire Mass Spectrometry." Journal of Biomolecular Screening 19, no. 4 (December 31, 2013): 508–15. http://dx.doi.org/10.1177/1087057113518069.

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Kynurenine 3-monooxygenase (KMO) is a therapeutically important target on the eukaryotic tryptophan catabolic pathway, where it converts L-kynurenine (Kyn) to 3-hydroxykynurenine (3-HK). We have cloned and expressed the human form of this membrane protein as a full-length GST-fusion in a recombinant baculovirus expression system. An enriched membrane preparation was used for a directed screen of approximately 78,000 compounds using a RapidFire mass spectrometry (RF-MS) assay. The RapidFire platform provides an automated solid-phase extraction system that gives a throughput of approximately 7 s per well to the mass spectrometer, where direct measurement of both the substrate and product allowed substrate conversion to be determined. The RF-MS methodology is insensitive to assay interference, other than where compounds have the same nominal mass as Kyn or 3-HK and produce the same mass transition on fragmentation. These instances could be identified by comparison with the product-only data. The screen ran with excellent performance (average Z′ value 0.8) and provided several tractable hit series for further investigation.

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