Jurgen Joossens

TL;DR: In this paper, the authors explored the structure-activity relationship around the core scaffold of the N-4-quinolinoyl-gly-(2S)-cyanoPro scaffold and reported extensively optimized compounds that display low nanomolar inhibitory potency and high selectivity against the related dipeptidyl peptidases (DPPs) DPPIV, DPP9, and prolyl oligopeptidase (PREP).

TL;DR: The discovery of a new class of FAP inhibitors with a N-(4-quinolinoyl)-Gly-(2-cyanopyrrolidine) scaffold is presented and the effects of substituting the quinoline ring and varying the position of its sp(2) hybridized nitrogen atom are explored.

TL;DR: The kinetics of binding, the type of inhibition, the selectivity with respect to other peptidases, and the inhibitory potency on the DPP IV catalyzed degradation of glucagon-like peptide-1 (GLP-1), glucose-dependent insulinotropic polypeptide (GIP) and substance P were reported.

TL;DR: The mechanisms by which proteases alter the intestinal permeability are outlined, including the role of proteases in mucosal homeostasis and gastrointestinal barrier function, which will definitely contribute to the identification of new therapeutic targets for permeability-related diseases.

TL;DR: The synthesis of novel ferroptosis inhibitors containing amide and sulfonamide moieties with improved stability, single digit nanomolar antiferroptotic activity, and good ADME properties suitable for application in in vivo disease models are reported.