Laure Guilhaudis

TL;DR: This work synthesized a series of URP analogs and measured their binding affinity on hGPR14-transfected cells and their contractile activity in a rat aortic ring bioassay to find the most potent antagonist in this series.

TL;DR: It is suggested that the N-terminal tail of PACAP adopts a specific conformation similar to a turn when it activates the PAC1 receptor, and this conformation could constitute an appropriate molecular scaffold supporting the design of nonpeptidic PAC1 receptors agonists.

TL;DR: Bicarinalin had a potent and broad antibacterial activity of the same magnitude as Melittin and other hymenopteran antimicrobial peptides such as Pilosulin or Defensin, suggesting potential for development into an anti-infective agent for use against emerging antibiotic-resistant pathogens.

TL;DR: Functional and structural analyses of a series of Ala-substituted rat kp-10 analogs suggest that modifications in these positions could lead to the generation of new kisspeptin agonists and/or antagonists with altered functional and perhaps binding properties, and emphasize the importance of using combined, multidisciplinary approaches to reliably evaluate structure function properties of novelkisspeptin analogs.

TL;DR: Structure-activity relationship studies provide crucial information regarding the structural and conformational requirements for ligand-receptor interactions, which will be of considerable importance for the design of novel UT ligands with increased selectivity, potency and stability, that may eventually lead to the development of innovative drugs.