Department of Pharmaceutical Sciences, COMSATS Institute of Information Technology, Abbottabad, Postal Code 22060, Pakistan.
Eur J Med Chem. 2011 Nov;46(11):5473-9. doi: 10.1016/j.ejmech.2011.09.009. Epub 2011 Sep 16.
A series of new and novel Schiff base derivatives were synthesized and investigated as potential new inhibitors of Jack bean urease. The most potent compounds were 3f with (K(i) = 0.09 μM) and 3k (K(i) = 0.122 μM). A pure competitive mechanism of inhibition was observed. Molecular docking studies were also performed to illustrate the binding mode of the compounds. Docking studies were performed on both enzymes from Jack bean urease and H. pylori urease. It was observed that both share the same binding mode. The binding sites of the two urease structures also aligned very well indicating the similarity in binding sites of the enzymes.
一系列新的和新颖的席夫碱衍生物被合成并研究为潜在的新型刀豆脲酶抑制剂。最有效的化合物是 3f（K(i) = 0.09 μM）和 3k（K(i) = 0.122 μM）。观察到纯竞争抑制机制。还进行了分子对接研究以说明化合物的结合模式。对接研究分别在刀豆脲酶和 H. pylori 脲酶的两种酶上进行。观察到它们具有相同的结合模式。两种脲酶结构的结合位点也非常吻合，表明酶的结合位点具有相似性。
