Portage Transport of Toxophoric Agent, N-hydroxyalanine, through Oligopeptide Permease in Escherichia coli

Di-and tri-peptides containing DL-N-hydroxyalanine were prepared. DL-N-Hydroxyalanine was linked, via its primary amino group, to the -carbon of glycine residues in dipeptide synthon (L-alanyl(-DL-N-hydroxyalanyl)DL-glycine) 5, and tripeptide synthon (L-alanyl-L-alanyl(-DL-N-hydroxyalanyl) DL-glycine) 12. 5 proved to be 19 times more potent than DL-N-hydroxyalanine when tested in vitro for the ability to inhibit the growth of E coli. However, 12 gave comparable potency to DL-N-hydroxyalanine itself.