A new series of 2,3-disubstituted quinazolin-4(3H)-one compounds including oxadiazole and furan rings was synthesized. Their inhibitory activities on urease were assessed in vitro. All newly synthesized compounds exhibited potent urease inhibitory activity in the range of IC₅₀ = 1.55 ± 0.07–2.65 ± 0.08 µg/mL, when compared with the standard urease inhibitors such as thiourea (IC₅₀ = 15.08 ± 0.71 µg/mL) and acetohydroxamic acid (IC₅₀ = 21.05 ± 0.96 µg/mL). 2,3-Disubstituted quinazolin-4(3H)-one derivatives containing furan ring (3a-e) were found to be the most active inhibitors when compared with the compounds 2a-e bearing oxadiazole ring. Compound 3a, bearing 4-chloro group on phenyl ring, was found as the most effective inhibitor of urease with the IC₅₀ value of 1.55 ± 0.11 µg/mL. The molecular docking studies of the newly synthesized compounds were performed to identify the probable binding modes in the active site of the Jack bean urease (JBU) enzymes.

合成了包括恶二唑和呋喃环在内的一系列新的2,3-二取代喹唑啉-4（3 H）-one化合物。评估了它们对脲酶的抑制作用。 与标准脲酶抑制剂（如硫脲）（IC ₅₀  = 15.08±0.71 µg / mL）和乙酰氧肟酸相比，所有新合成的化合物均表现出有效的尿素酶抑制活性，IC ₅₀ = 1.55±0.07–2.65±0.08 µg / mL。酸（IC ₅₀  = 21.05±0.96 µg / mL）。与化合物2a-e相比，发现含有呋喃环（3a-e）的2,3-二取代喹唑啉-4（3 H）-one衍生物是活性最高的抑制剂。带有恶二唑环。已发现在苯环上带有4-氯基的化合物3a是最有效的脲酶抑制剂，IC ₅₀值为1.55±0.11 µg / mL。进行了对新合成化合物的分子对接研究，以鉴定在杰克豆脲酶（JBU）酶的活性位点中可能的结合方式。