Study of cracks propagation inside the steel on press hardened steel zinc based coatings

Al-Si coating is the most suitable solution for main Hot-Forming applications, particularly in terms of processwindow for the hot stampers and in perforating corrosion resistance after austenitization. But for some specificcases, a few customers require galvanic edge protection. So, in order to satisfy this requirement zinc basedcoatings were developed for Hot-Forming.On these Zn based coatings a full microstructural characterization was carried out on the coating influence onthe steel/coating interface during the hot stamping. It appears that some cracks propagation is alwaysobserved inside the steel with Zn based coatings. Two separate cases corresponding to two mechanisms have tobe distinguished: Macro and Micro-cracks. The MACRO-cracks propagation is related to a liquid zincpenetration inside the previous austenitic steel grains boundaries. This is encountered for areas showing ahigh level of tensile stress with remaining liquid Fe-Zn phases in the coating during the deformation. Thus, acold deformation is a preliminary step for GI coating. The MICRO-cracks propagation is related to a frictionissue between the coating surface and the tools at high temperature. The higher micro-cracks density isconsequently observed on areas more sensitive to friction. The phases inside the steel responsible for thispropagation have been identified. Some solutions to avoid these phenomena are proposed, particularly in thecase of the micro-cracks for Direct Hot-Forming applications (GA coatings)

Discovery of the First in Vivo Active Inhibitors of the Soluble Epoxide Hydrolase Phosphatase Domain

The emerging pharmacological target soluble epoxide hydrolase (sEH) is a bifunctional enzyme exhibiting two different catalytic activities that are located in two distinct domains. Although the physiological role of the C-terminal hydrolase domain is well-investigated, little is known about its phosphatase activity, located in the N-terminal phosphatase domain of sEH (sEH-P). Herein we report the discovery and optimization of the first inhibitor of human and rat sEH-P that is applicable in vivo. X-ray structure analysis of the sEH phosphatase domain complexed with an inhibitor provides insights in the molecular basis of small-molecule sEH-P inhibition and helps to rationalize the structure-activity relationships. 4-(4-(3,4-Dichlorophenyl)-5-phenyloxazol-2-yl)butanoic acid (22b, SWE101) has an excellent pharmacokinetic and pharmacodynamic profile in rats and enables the investigation of the physiological and pathophysiological role of sEH-P in vivo