Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Portage Transport of Toxophoric Agent, N-hydroxyalanine, through Oligopeptide Permease in Escherichia coli

  • Hong, Nam-Joo (Department of Applied Microbiology, College of Agriculture, Yeungnam University) ;
  • Park, Yeong-Taek (Department of Applied Microbiology, College of Agriculture, Yeungnam University)
  • Published : 1993.12.20
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Abstract

Di-and tri-peptides containing DL-N-hydroxyalanine were prepared. DL-N-Hydroxyalanine was linked, via its primary amino group, to the ${\alpha}$-carbon of glycine residues in dipeptide synthon (L-alanyl(${\alpha}$-DL-N-hydroxyalanyl)DL-glycine) 5, and tripeptide synthon (L-alanyl-L-alanyl(${\alpha}$-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.

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