Inhibition of jack bean urease by amphiphilic peptides

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 ( 1 H and 13 C-NMR) and in vitro urease inhibitory activity of amphiphilic peptides was studied. Amphiphilic peptides 12 and 33 showed excellent urease inhibitory activity, ( p