Prof. Dr. Joachim Jose

© Dziemba

Topics of research

Autodisplay, bacterial surface display of recombinant proteins and applications in:
• Assay development and inhibitor testing
• Whole cell biocatalysts for synthesis of drugs and building blocks
• Directed evolution of enzyme inhibitors and biocatalysts
• Biosensor development and diagnostic tools

ChemBIon project description

ChemBIon project descriptions
Autodisplay of the NMDAR GluN1/2A ligand binding domains
More recently, the ligand binding domains (LBDs) of GluN1 and of GluN2A were expressed in soluble form in E. coli and were shown to form functional dimers, again proven by kinetic studies. Co-crystallization experiments unveiled the binding mode of negative allosteric modulators (NAMs) e.g. TCN-201, which address a pocket, formed at the interface of both subunits. Conformational changes after binding the agonists glutamate and glycine with or without NAMs provided a clear concept for the observed allosteric inhibition of NMDAR. Objective: The goal of this project is a) the co-expression of the LBDs of GluN1 and GluN2A on the bacterial cell surface and b) to show the functionality by kinetic studies with known compounds. This will enable c) to establish a new screening method for antagonists and negative allosteric modulators of NMDAR by a fluorescence derivative of TCN-201.
MST based assay for HCN channel activator identification
Microscale thermophoresis (MST) is a new method for the rapid measuring of KD values of two binding partners in µL solutions.3 The motion of molecules within a temperature gradient is called Ludwig-Soret-effect or thermophoresis. MST determines the different motion of a molecule with or without bound ligand within a moderate temperature gradient between 23 -25°C, which is induced by an IR laser beam. For this purpose, different concentrations of the ligand are added to a fixed concentration of the fluorescence labelled binding partner, and for each concentration the thermophoresis is determined. The resulting curve, thermophoresis in dependence of ligand concentration, yields the binding constant. Using this strategy, KD values can be determined with minimal amounts of binding partners within minutes. More recently, we could show that human target proteins can be labelled by click chemistry and used in soluble or surface displayed form for the determination of protein-small molecule interactions and protein-protein interactions
Objective: The aim of this project is the development of a rapid screening assay for HCN4 channel activators using microscale thermophoresis (MST) based assay.

  • Curriculum vitae

    1981 - 1989

    Studies of Biology at Saarland University, Saarbrücken


    Promotion to a Dr. rer. nat. (magna cum laude) at the Institute of Microbiology in the group of H. Kaltwasser

    1994 - 1997

    Postdoc, Max-Planck-Institute (MPI) for Biology, Tübingen and the MPI for Infection Biology, Berlin (Thomas F. Meyer)

    1997 - 1998

    Postdoc, Institute of Pharmaceutical and Medicinal Chemistry, University Saarbrücken (Rolf W. Hartmann)

    1998 - 2004

    Research associate (C1) and Group Leader, Institute of Pharmaceutical and Medicinal Chemistry, University Saarbrücken


    Co-Founder and Shareholder Pharmacelsus GmbH, Germany, Contract Research Organization for Preclinical studies and Absorption Screening.

    2003 - 2004

    Priv.-Dozent, Institute of Pharmaceutical and Medicinal Chemistry, University Saarbrücken

    2004 - 2011

    Associate Professor (C3) for Bioanalytics, Institute of Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universiy (HHU) Düsseldorf


    Cofounder, CSO and Shareholder Auodisplay Biotech GmbH, Start-Up Company in the field of Biocatalysis and Screening Systems.

    since 2011

    Full Professor (W3) for Pharmaceutical and Medicinal Chemistry at the PharmaCampus, Westfälische Wilhelms-University (WWU) Münster