Laura Depta, M. Sc.

Position: PhD Student

Room no.: CP-02-112

Telephone no.: +49 231 755 7056

Member of the group since: 11/2018

University Degree: M. Sc. in Chemical Biology, TU Dortmund University


Expertise: organic synthesis, biochemical and-physical methods, protein expression and purification, protein crystallization

Off-Lab activities (hobbies): athletics and weight lifting, reading, cooking

Research projects:

The protein kinases Akt1, Akt2, and Akt3 are highly conserved regulators within cellular signaling networks. They are involved in many processes such as proliferation, survival, and metabolism. Currently, the individual roles of the different isoforms in disease states are not completely understood, so there is a strong need for pharmacological perturbation studies to dissect the functional role of the individual Akt isoforms. We want to develop covalent-allosteric inhibitors with an ideal selectivity profile towards Akt isoforms and further functionalize those as potent probes, to eventually allow for the dissection of the biological functions of Akt1, Akt2, and Akt3.

Crystallization studies of the three isoforms revealing the covalent bond formation and validating the predicted binding mode, are essential to provide opportunities for further compound optimization. Also a strong focus of my project lies on the evaluation of these compounds in different cancer cell lines.


Earlier positions:

Bachelor and Master studies at Rauh group on synthesis and evaluation of allosteric kinase modulators and synthesis and evaluation of stapled peptides



  1. Landel, I.; Quambusch, L.; Depta, L.; Rauh, D.. Spotlight on AKT: Current Therapeutic Challenges. ACS Med. Chem. Lett. 2020, 11 (3), 225–227.

    DOI PubMed

  2. a) Quambusch, L.; Landel, I.; Depta, L.; Weisner, J.; Uhlenbrock, N.; Müller, M. P.; Glanemann, F.; Althoff, K.; Siveke, J. T.; Rauh, D.. Covalent-Allosteric Inhibitors to Achieve Akt Isoform-Selectivity. Angew. Chem. Int. Ed. Engl. 2019, 58 (52), 18823–18829.

    DOI PubMed

    b) Quambusch, L.; Landel, I.; Depta, L.; Weisner, J.; Uhlenbrock, N.; Müller, M. P.; Glanemann, F.; Althoff, K.; Siveke, J. T.; Rauh, D.. Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity. Angew. Chem. 2019, 131 (52), 18999–19005.


  3. Uhlenbrock, N.; Smith, S.; Weisner, J.; Landel, I.; Lindemann, M.; Le, T. A.; Hardick, J.; Gontla, R.; Scheinpflug, R.; Czodrowski, P.; Janning, P.; Depta, L.; Quambusch, L.; Müller, M. P.; Engels, B.; Rauh, D.. Structural and chemical insights into the covalent-allosteric inhibition of the protein kinase Akt. Chem. Sci. 2019, 10 (12), 3573–3585.

    DOI PubMed

  4. Weisner, J.; Landel, I.; Reintjes, C.; Uhlenbrock, N.; Trajkovic-Arsic, M.; Dienstbier, N.; Hardick, J.; Ladigan, S.; Lindemann, M.; Smith, S.; Quambusch, L.; Scheinpflug, R.; Depta, L.; Gontla, R.; Unger, A.; Müller, H.; Baumann, M.; Schultz-Fademrecht, C.; Günther, G.; Maghnouj, A.; Müller, M. P.; Pohl, M.; Teschendorf, C.; Wolters, H.; Viebahn, R.; Tannapfel, A.; Uhl, W.; Hengstler, J. G.; Hahn, S. A.; Siveke, J. T.; Rauh, D.. Preclinical Efficacy of Covalent-Allosteric AKT Inhibitor Borussertib in Combination with Trametinib in KRAS-Mutant Pancreatic and Colorectal Cancer. Cancer Res. 2019, 79 (9), 2367–2378.

    DOI PubMed