Prof. Dr. Dietrich Volmer

Profil

Zusammenfassung

Prof. Volmer entwickelt analytische Methoden zur Charakterisierung komplexer biologischer Moleküle, insbesondere mit Massenspektrometrie. Seine Expertise umfasst die Optimierung von Probenvorbereitung, die Quantifizierung schwer messbarer Substanzen (wie Vitamin-D-Metaboliten) in biologischen Proben und innovative Ionisierungstechniken. Diese Methoden ermöglichen es, Biomarker für Krankheitsdiagnose und Therapiemonitoring zuverlässig zu bestimmen.

Skills

Name

Prof. Dr. Dietrich Volmer

Titel

Prof. Dr.

Fakultät

Mathematisch-Naturwissenschaftliche Fakultät

Institut

Institut für Chemie

Arbeitsgruppe

Angewandte Analytik und Umweltchemie

E-Mail

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Telefon

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HU-FIS-Profil

Quelle ↗

Zuletzt gescrapt

27.6.2026, 01:16:01

• Einsatz der akustischen Levitation zur Etablierung einer vollständig integrierten "Lab-in-a- Droplet"-Plattform: Kombination von in stillo Probenvorbereitung und direkter massenspektrometrischer Analyse

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 02/2026 - 01/2029 Projektleitung: Prof. Dr. Dietrich Volmer

• Ein systemischer Ansatz zur Charakterisierung von Vitamin D: Ausdehnung der massenspektrometrischen Analytik auf Gewebe, als Ergänzung zu Serum-Vitamin D

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 06/2026 - 05/2029 Projektleitung: Prof. Dr. Dietrich Volmer, Prof. Dr. Caroline Stokes

• Ein systemischer Ansatz zur Charakterisierung von Vitamin D: Ausdehnung der massenspektrometrischen Analytik auf Gewebe, als Ergänzung zu Serum-Vitamin D

  Quelle ↗

  Förderer: DFG Eigene Stelle (Sachbeihilfe) Zeitraum: 07/2026 - 06/2029 Projektleitung: Prof. Dr. rer. nat. Dr. rer. agr. Christian Ulrichs, Prof. Dr. Dietrich Volmer

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• Ion activation methods for tandem mass spectrometry

  2004

  Journal of Mass Spectrometry · 512 Zitationen · 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.

• Recent advances in sample preparation techniques to overcome difficulties encountered during quantitative analysis of small molecules from biofluids using LC-MS/MS

  2014

  The Analyst · 266 Zitationen · 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.

• Lipid imaging by mass spectrometry – a review

  2012

  The Analyst · 212 Zitationen · 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.

• Charité – Universitätsmedizin Berlin

  Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS

  university

• Max-Delbrück-Centrum für Molekulare Medizin

  Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS

  other

• Max-Planck-Institut für molekulare Genetik

  Multimodale klinische Massenspektrometrie für die Untersuchung von Therapieresistenz - MSTARS

  other