Scientists from the Physikalisch-Technische Bundesanstalt (PTB) have implemented a novel pressure measurement method, quasi as a byproduct of the work on the "new" kelvin. In addition to being new, this procedure is a primary method, i.e. it only depends on natural constants. As an independ ... more
Dr. André Henrion
Physikalisch-Technische Bundesanstalt (PTB)
André Henrion, born in 1957, studied chemistry at Humboldt-University in Berlin, where he received his doctorate in 1988 in the field of Physical Organic Chemistry. After working at the Academy of Sciences in Berlin for a short period he moved on to the Physikalisch-Technische Bundesanstalt (PTB) in 1992. Since 2001 he has been Head of Working Group Bioorganic Mass Spectrometry as part of the Biochemistry Group within PTB.
Resulting from his scope of tasks at the PTB the activities of André Henrion are mainly focused on the quantitative analysis of diagnostic and therapeutic markers by mass spectrometry. Corresponding with recent developments in the area, his focus has shifted over the last 15 years from quantification of small organic molecules to peptides and proteins as analytical targets. Beyond this, needing to interpret large amounts of generated data has led to statistics, chemometrics and bioinformatics becoming further areas of his expertise. André Henrion has represented the PTB for over 20 years in the Organic Analysis and Protein Analysis Working Groups in BIPM (CCQM), is a member of the Working Group on Immunosuppressive Drugs within the Scientific Division of the IFCC and leads a Review Team at the Joint Committee for Traceability in Laboratory Medicine (JCTLM). He has co-authored 42 original works, four reviews or book chapters and a monograph.
André Henrion received the Emil-Fischer-Award of Humboldt-University Berlin in 1983 and a Best Paper Award of the Cooperation on International Traceability in Analytical Chemistry (CITAC) in 2010.
The Working Group of André Henrion mainly uses quantitative bottom-up (shotgun-) proteomics for the targeted quantification of proteins in clinical or biological samples. For the most accurate results, isotope labeled peptides or recombinant proteins are referred to as sources for internal standards. Complementary, label-free methods are being developed for the quantification of entire spectra of proteins (within proteomes) to allow for e.g. purity-determination of reference materials, making them potentially applicable for purity-monitoring of pharmaceutical products or for process control. Another area of interest is developing cross-linking mass spectrometry (XL-MS) to characterize protein-tertiary structures and protein-protein interactions.
- Analytical mass spectrometry
- Chemometrics, bioinformatics