au1235 and Pancreatitis

au1235 has been researched along with Pancreatitis* in 2 studies

Other Studies

2 other study(ies) available for au1235 and Pancreatitis

ArticleYear
From the Design to the
    Journal of medicinal chemistry, 2021, 05-13, Volume: 64, Issue:9

    The pharmacological inhibition of soluble epoxide hydrolase (sEH) is efficient for the treatment of inflammatory and pain-related diseases. Numerous potent sEH inhibitors (sEHIs) present adamantyl or phenyl moieties, such as the clinical candidates AR9281 or EC5026. Herein, in a new series of sEHIs, these hydrophobic moieties have been merged in a benzohomoadamantane scaffold. Most of the new sEHIs have excellent inhibitory activities against sEH. Molecular dynamics simulations suggested that the addition of an aromatic ring into the adamantane scaffold produced conformational rearrangements in the enzyme to stabilize the aromatic ring of the benzohomoadamantane core. A screening cascade permitted us to select a candidate for an

    Topics: Acute Disease; Adamantane; Animals; Binding Sites; Catalytic Domain; Cell Membrane Permeability; Drug Design; Drug Stability; Enzyme Inhibitors; Epoxide Hydrolases; Half-Life; Humans; Hydrophobic and Hydrophilic Interactions; Male; Mice; Mice, Inbred C57BL; Molecular Dynamics Simulation; Pancreatitis; Rats; Structure-Activity Relationship

2021
2-Oxaadamant-1-yl Ureas as Soluble Epoxide Hydrolase Inhibitors:
    Journal of medicinal chemistry, 2020, 09-10, Volume: 63, Issue:17

    Topics: Acute Disease; Animals; Binding Sites; Catalytic Domain; Cell Line; Cell Survival; Disease Models, Animal; Endoplasmic Reticulum Stress; Enzyme Inhibitors; Epoxide Hydrolases; Half-Life; Humans; Mice; Microsomes; Molecular Dynamics Simulation; Pancreatitis; Rats; Solubility; Structure-Activity Relationship; Urea

2020