Prof. Volmer entwickelt und wendet hochauflösende Massenspektrometrie-Verfahren an, um komplexe biologische und Umweltproben zu analysieren. Sein aktueller Schwerpunkt liegt auf der Charakterisierung von Vitamin-D-Metaboliten in Serum und Geweben sowie auf innovativen Analysemethoden wie der akustischen Levitation für miniaturisierte Probenvorbereitung (Lab-in-a-Droplet). Parallel arbeitet er an massenspektrometrischen Techniken zur Untersuchung von Therapieresistenz in der Klinik, zur Detektion von Umweltschadstoffen (Reifenchemikalien, organische Schadstoffe in Wasser und Luft) und zur Quantifizierung von Lignin in Biomaterialien. Seine Methoden ermöglichen es Kliniken und Umweltlaboren, niedrig konzentrierte, dynamische Stoffe schneller und präziser zu erfassen — relevant für Diagnostik, Pharmaforschung, Umweltmonitoring und Materialwissenschaften.
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Prof. Dr. Dietrich Volmer
HU-FIS-Profil ↗Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS
university
Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS
other
Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS
other
Förderer: DFG Sachbeihilfe Zeitraum: 01/2020 - 02/2024 Projektleitung: Prof. Dr. Dietrich Volmer
Förderer: Bundesministerium für Forschung, Technologie und Raumfahrt Zeitraum: 03/2020 - 02/2023 Projektleitung: Prof. Dr. Dietrich Volmer
Förderer: DFG Sachbeihilfe Zeitraum: 07/2020 - 09/2024 Projektleitung: Prof. Dr. Dietrich Volmer
Journal of Mass Spectrometry · DOI
This tutorial presents the most common ion activation techniques employed in tandem mass spectrometry. In-source fragmentation and metastable ion decompositions, as well as the general theory of unimolecular dissociations of ions, are initially discussed. This is followed by tandem mass spectrometry, which implies that the activation of ions is distinct from the ionization step, and that the precursor and product ions are both characterized independently by their mass/charge ratios. In collision-induced dissociation (CID), activation of the selected ions occurs by collision(s) with neutral gas molecules in a collision cell. This experiment can be done at high (keV) collision energies, using tandem sector and time-of-flight instruments, or at low (eV range) energies, in tandem quadrupole and ion trapping instruments. It can be performed using either single or multiple collisions with a selected gas and each of these factors influences the distribution of internal energy that the activated ion will possess. While CID remains the most common ion activation technique employed in analytical laboratories today, several new methods have become increasingly useful for specific applications. More recent techniques are examined and their differences, advantages and disadvantages are described in comparison with CID. Collisional activation upon impact of precursor ions on solid surfaces, surface-induced dissociation (SID), is gaining importance as an alternative to gas targets and has been implemented in several different types of mass spectrometers. Furthermore, unique fragmentation mechanisms of multiply-charged species can be studied by electron-capture dissociation (ECD). The ECD technique has been recognized as an efficient means to study non-covalent interactions and to gain sequence information in proteomics applications. Trapping instruments, such as quadrupole ion traps and Fourier transform ion cyclotron resonance instruments, are particularly useful for the photoactivation of ions, specifically for fragmentation of precursor ions by infrared multiphoton dissociation (IRMPD). IRMPD is a non-selective activation method and usually yields rich fragmentation spectra. Lastly, blackbody infrared radiative dissociation is presented with a focus on determining activation energies and other important parameters for the characterization of fragmentation pathways. The individual methods are presented so as to facilitate the understanding of each mechanism of activation and their particular advantages and representative applications.
The Analyst · DOI
Liquid chromatography-mass spectrometry analysis of small molecules from biofluids requires sensitive and robust assays. Because of the very complex nature of many biological samples, efficient sample preparation protocols to remove unwanted components and to selectively extract the compounds of interest are an essential part of almost every bioanalytical workflow. This review describes the most common problems encountered during sample preparation, ways to optimize established sample preparation techniques and important recent developments to reduce or eliminate major interferents from biofluids.
The Analyst · DOI
Mass spectrometry imaging (MSI) has proven to be extremely useful for applications such as the spatial analysis of peptides and proteins in biological tissue, the performance assessment of drugs in vivo or the measurement of protein or metabolite expression as tissue classifiers or biomarkers from disease versus control tissue comparisons. The most popular MSI technique is MALDI mass spectrometry. First invented by Richard Caprioli in the mid-1990s, it is the highest performing MSI technique in terms of spatial resolution, sensitivity for intact biomolecules and application range today. The unique ability to identify and spatially resolve numerous compounds simultaneously, based on m/z values has inter alia been applied to untargeted and targeted chemical mapping of biological compartments, revealing changes of physiological states, disease pathologies and metabolic faith and distribution of xenobiotics. Many MSI applications focus on lipid species because of the lipids' diverse roles as structural components of cell membranes, their function in the surfactant cycle, and their involvement as second messengers in signalling cascades of tissues and cells. This article gives a comprehensive overview of lipid imaging techniques and applications using established MALDI and SIMS methods but also other promising MSI techniques such as DESI.