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A series of N‐arylalkanyl 2‐naphthamides (Xa~e), which were predicted from virtual molecular docking on a built xanthine oxidase template as potential inhibitors, were synthesized. Their inhibitory activity against xanthine oxidase was assayed. Among these prepared, compounds Xb (IC50 13.6 μM), Xc (IC50 13.1 μM), and Xd (IC50 12.5 μM) showed comparable inhibitory activity to allopurinol (IC50 22.1 μM). The in vitro assay result correlated well with molecular docking scores, ΔG = −16.99, −17.66, and −17.13 Kcal/mol, respectively. On the potassium oxonate‐induced hyperuricemic mice model, oral administration of Xc‐Ac (40 mg/ Kg), the per‐O‐acetylated Xc, could reduce the blood uric acid level by 60% in comparison to the normal control group and is statistically significant (p <.01) while compared with the hyperuricemic mice group. [ABSTRACT FROM AUTHOR]

SaeR is the response regulator of the SaeRS two-component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N-terminal receiver domain and a C-terminal effector domain. The effector domain possesses DNA-binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P212121, with unit-cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding. [ABSTRACT FROM AUTHOR]