Fakultät für Chemie - Former
 
 
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Bielefeld University > Department of Chemistry > Organic Chemistry III > Team > Former

Personal data for Michael Hoefener

  Michael Hoefener
Michael Hoefener
PhD student
Room: F2-246
Phone: 0521 106 2145
E-Mail:

Molecular tools for functional proteomics and interactomics


The p38 MAPK is an important activator for a number of signaling pathways. Hence, it is involved in various disorders such as ovarian cancer, rheumatoid arthritis, Crohn?s disease and psoriasis. Due to the low abundance of MAPKs, especially the p38 family classical tools for proteomics are not useful to investigate those proteins.

During the past years affinity based proteomics was successfully applied to investigate low abundant proteins in complex mixtures on the one hand and for evaluation of protein inhibitors on the other. In order to get a better understanding of the p38 kinases and their signaling pathways, small molecules suitable for inhibitor affinity chromatography need to be synthesized. This method employs synthetic probes which contain a reversibly binding inhibitor immobilized to a solid phase. Low abundant proteins can be captured from crude material and identified via LC-MS-MS analysis.

To investigate low abundant kinases such as the p38 family as well as to evaluate for example kinase inhibitors, powerfull probes for inhibitor affinity chromatography are required. Our current focus is therefore the synthesis of kinase probes suitable for inhibitor affinity chromatography.