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Institut für Pharmazeutische Biologie und Biotechnologie

Herzlich Willkommen auf den Seiten des Instituts für Pharmazeutische Biologie und Biotechnologie der Heinrich Heine Universität Düsseldorf.

 

News

Fostering the 3R concept in drug discovery

24.04.2024

On April 24th Nicole Teusch had the pleasure of presenting a new 3D organoid-on-chip model developed in collaboration with Dynamic42 GmbH to the scientific advisory board of the set foundation (Foundation for the Promotion of Research on Alternative Methods to Animal Experiments).

An inspiring afternoon with many exciting discussions and new ideas on modern alternative methods in pharmaceutical research.

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Contribution to an invited review on bacterial α-glucan metabolism published in Chemical Reviews

24.04.2024

See our recent contribution to an invited review article entitled “Architecture, function, regulation and evolution of α-glucans metabolic enzymes in prokaryotes” published in Chemical Reviews, which is one of the highest-ranked journals covering general topics of chemistry (IF 62.1). This review was written by Rainer Kalscheuer in collaboration  with colleagues from the University of the Basque Country, the Molecular Biology Institute of Barcelona (IBMB), and the University of Lille.

 

Original publication:

Cifuente JO, Colleoni C, Kalscheuer R, Guerin ME. Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes. Chem Rev. (2024) online ahead of print  (doi: 10.1021/acs.chemrev.3c00811).

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Contribution of the Kalscheuer lab to a study advancing the homo-BacPROTAC concept as new antimycobacterial treatment option published in Nature Communications

05.03.2024

See our recent contribution to a study advancing the homo-BacPROTAC concept as new antimybacterial treatment option published in Nature Communications. This study was conducted in collaboration with Guido Boehmelt and coworkers at Boehringer Ingelheim RCV, Vienna, Austria, Lukas Junk at Saarland University, and further colleagues.

Homo-BacPROTACs consist of two cyclomarin A-molecules, which both can bind separate ClpC1 proteins. ClpC1 represents the mycobacterial ATP-driven unfoldase of the quasi-proteasomal like ClpC:ClpP (ClpCP) protease. Homo-BacPROTACs induce proximity between separate ClpC1 proteins, which results in selfdegradation of ClpC1 and impairs activity of the Clp protein quality control system. This innovative technology may provide a new way to tackle the rising problem of antimicrobial resistance in the human pathogen Mycobacterium tuberculosis.

 

Original publication:

Junk L*, Schmiedel VM*, Guha S, Fischel K, Greb P, Vill K, Krisilia V, van Geelen L, Rumpel K, Kaur P, Krishnamurthy RV, Narayanan S, Shandil RK, Singh M, Kofink C, Mantoulidis A, Biber P, Gmaschitz G, Kazmaier U, Meinhart A, Leodolter J, Hoi D, Junker S, Morreale FE, Clausen T, Kalscheuer R, Weinstabl H, Boehmelt G. Homo-BacPROTAC-induced degradation of ClpC1 as a strategy against drug-resistant mycobacteria. Nat Commun 15, 2005 (2024). https://doi.org/10.1038/s41467-024-46218-7

*These authors contributed equally. 

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