Claudia Henn

TL;DR: An overview of functional and structural aspects for the different 17β-HSDs is given and the selective inhibition of the concerned enzymes might provide an effective treatment and a good alternative to the existing endocrine therapies.

TL;DR: In vitro evaluation using a reporter gene assay in Escherichia coli led to the discovery of the first competitive PqsR antagonists, which are highly potent (K(d,app) of compound 20: 7 nM).

TL;DR: The identified PqsR antagonists are promising scaffolds for further drug design efforts against this important pathogen and provide insights into the energetic characteristics of protein-ligand interactions.

TL;DR: Site-directed mutagenesis in combination with isothermal titration calorimetry and NMR INPHARMA experiments revealed that the identified ligands bind to the same site of PqsR by adopting different binding modes, which will be utilized in a future fragment-growing approach aiming at novel therapeutic options for the treatment of P. aeruginosa infections.

TL;DR: Inhibition of 17β-HSD1 inhibitors from the hydroxyphenylnaphthol class by introduction of different heteroaromatic rings as well as substituted phenyl groups showed a good membrane permeation and metabolic stability and was orally available in the rat.