7th CONFERENCE OF THE CZECH SOCIETY FOR MASS SPECTROMETRY - BOOK OF ABSTRACTS

Significance of the Topic
Mass spectrometry (MS) is pivotal in analytical chemistry for characterizing small molecules, peptides, proteins, and complex biological samples. Its capabilities enable detailed molecular profiling vital in drug discovery, clinical diagnostics, environmental monitoring, and biotechnological research.

C-Term Goals and Study Overview
This summary covers key developments from the Seventh Annual Conference of the Czech Society for Mass Spectrometry (Prague, April 2018). It outlines advances in instrumentation, emerging methodologies, and applications in proteomics, metabolomics, and gas-phase reaction studies.

Study Methodology and Instrumentation
• Ionization Techniques: ESI, APCI, MALDI, nanoDESI, micro-APCI, DESI.
• High-Resolution MS Platforms: Q-TOF, Orbitrap, FT-ICR, Triple Quadrupole MS.
• Chromatography: LC-MS/MS, GCxGC-MS, SFC-MS, SEC-MS.
• Ion Mobility: Trapped ion mobility spectrometry (TIMS) and PASEF.
• Structural MS: H/D exchange, cross-linking, IR photodissociation.
• Sample Preparation: Microgradient fractionation, Filter Aided Sample Preparation (FASP), glycan permethylation, solid-phase enrichments.

Main Results and Discussion
1. Gas-Phase and Catalysis Studies
• Helmut Schwarz: Gas-phase single-atom catalysis with Au, Ta, Pt complexes revealing unique C–C, C–N bond formations at single-collision conditions.
• František Tureček: Generation and spectroscopic characterization of nucleotide and peptide radicals via electron transfer and intramolecular oxidation.
• Andris & Navrátil: Preparation and reactivity of terminal iron nitrides and iron(III)-oxo species in the gas phase, obtaining Fe–O stretching frequencies and mechanistic insights.

2. Proteomics Advances
• PASEF on TIMS-QTOF enables >130 MS/MS/s, identifying 15,000 peptides from 12 ng HeLa digest.
• nanospray APCI source and GDVN sprayer for sub-µL/min ionization of nonpolar analytes.
• Conventional-flow LC-MS at µL/min for exploratory proteomics achieved comparable coverage to nanoLC by optimizing columns, flow, temperature, and mobile phase.
• HDX-MS and cross-linking to map antibody epitopes, chaperone allostery (Hsp70), and TEAD1–DNA interactions identify structural and dynamic changes.
• CRISPR-Cas9 TMEM70 knockout cells combined with LFQ and SILAC quantitative MS elucidate ATP synthase disorders.
• Label-free quantitative proteomics of bacterial virions (M-PMV, Cronobacter) and mitochondrial membranes identify host–pathogen interactions and assembly factors.

3. Metabolomics and Clinical Markers
• DIA in metabolomics surpasses DDA in MS/MS coverage; variable window DIA increased identified metabolites by ~70%.
• Profiling tryptophan-derived microbial metabolites and infl ammatory proteins in biofluids using HR/AM MS and targeted SRM quantifies biomarkers linked to immune response.
• Glyoxal ion chemistry with H3O+, NO+, O2•+ in SIFT-MS—identification of protonated formaldehyde and adduct ions; humidity effects and kinetic modeling.
• New UHPLC-MS/MS assays for autism spectrum disorder markers in urine; simultaneous quantification of nine metabolites.
• Tea pesticide analysis by QuEChERS extraction and Agilent Q-TOF LC/MS detects banned pesticides (methoprotryne, dioxacarb).

4. Imaging MS and Tissue Analysis
• MALDI-MS imaging with DAN for lipid mapping and Alzheimer’s plaque studies; optimization of sublimation vs. spraying (ImagePrep vs. iMatrixSpray).
• NanoDESI and micro-APCI-MS for lipid and small-molecule imaging and solution-phase analysis; custom inlet designs for low-flow ionization.
• MALDI imaging and confocal microscopy correlate perifosine distribution and spheroid viability in colorectal carcinoma models.

5. Glycomics and Lipidomics
• Permethylated N-glycan fractionation by RP microgradient and MALDI-TOF/TOF, detecting high-mass multiantennary glycans up to m/z 6300.
• GCxGC/TOFMS to study deuterium-labeled fatty acid biosynthesis in adipose tissue.
• HPLC-APCI-MS for FAMEs with temperature-programmed column gradient; micro-APCI shows 100× better sensitivity than conventional APCI.

Benefits and Practical Applications
• Enhanced sensitivity, speed, and specificity in proteome and metabolome coverage; enables studies on limited sample amounts.
• Novel MS interfaces (PASEF, micro-APCI, nanoDESI) expand analyte range and throughput.
• Structural MS techniques (HDX, cross-linking, ion spectroscopy) provide dynamic and mechanistic insights inaccessible to traditional methods.
• Integrated untargeted/targeted MS improves biomarker discovery and validation workflows.
• Advanced imaging MS informs drug distribution, tissue biochemistry, and pathology mapping.

Future Trends and Potential Applications
• Wider adoption of PASEF and ion mobility for single-cell proteomics and real-time diagnostics.
• Integration of HR-MS, DIA, AI-driven data analysis for deeper metabolome exploration and pathway elucidation.
• MS-based assays for liquid biopsy, noninvasive disease monitoring, early detection in oncology, neurology, and infectious diseases.
• Miniaturized MS and ambient ionization techniques for in situ environmental and clinical analysis.
• Continued development of biochemical probes and reporters for reactive intermediates, radicals, and transient species.

Conclusion
Mass spectrometry is rapidly advancing through innovations in ionization, separation, detection, and structural probes. These developments dramatically enhance the depth, speed, and breadth of molecular analysis across chemistry, biology, and medicine. The integration of quantitative, structural, and imaging MS workflows promises transformative applications from fundamental mechanistic studies to real-time diagnostics and precision medicine.

References
Key cited works are those of Schwarz (Angew. Chem. Int. Ed. 2015), Meier et al. (J. Proteome Res. 2015), Xu et al. (Anal. Chem. 2005), DePonte et al. (J. Phys. D Appl. Phys. 2008), Megerle et al. (Phys. Chem. Chem. Phys. 2011), Gañán-Calvo et al. (J. Aerosol Sci. 1999), Lodine et al. (Cell Host Microbe 2007), Byrdwell (Lipids 2001), Gilar et al. (J. Sep. Sci. 2005).