In the current study, amphiphilic peptides were designed and screened against Jack bean urease by using computer aided drug discovery approach. The result showed that out of thirty-eight amphiphilic peptides 1, 3, 12, 18, 30, and 33 exhibit stronger binding affinity with the active site of the enzyme through chelation of charged amino acids with the nickel ions i.e., Ni⁺² 841 and Ni⁺² 842 as well as hydrophobic contacts of the nonpolar tail with the nonpolar residues in the active site. The selected amphiphilic peptides were synthesized by solid-phase peptide synthesis strategy, characterized by fast atomic bombardment mass spectroscopy (FAB-MS) and nuclear magnetic resonance spectroscopy (¹H and ¹³C-NMR) and in vitro urease inhibitory activity of amphiphilic peptides was studied. Amphiphilic peptides 12 and 33 showed excellent urease inhibitory activity, (p < 0.001) with IC₅₀ values 20.5 ± 0.01, and 28.1 ± 0.03 µM respectively, which was considerably better than thiourea used as positive control.

在当前的研究中，通过使用计算机辅助药物发现方法设计和筛选了两亲性肽以对抗杰克豆脲酶。结果表明，在 38 种两亲性肽中， 1、3、12、18、30和33通过带电氨基酸与镍离子即 Ni ⁺² 841 的螯合而表现出与酶活性位点更强的结合亲和力。和 Ni ⁺² 842 以及非极性尾部与活性位点中的非极性残基的疏水接触。选定的两亲性肽通过固相肽合成策略合成，通过快速原子轰击质谱 (FAB-MS) 和核磁共振谱 ( ¹ H 和¹³ C-NMR)和两亲性肽的体外脲酶抑制活性进行了研究。两亲性肽12和33显示出优异的脲酶抑制活性 ( p  < 0.001)，IC ₅₀值分别为 20.5 ± 0.01 和 28.1 ± 0.03 µM，明显优于用作阳性对照的硫脲。