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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 14, Number 6
BKCSDE 14(6)
June 20, 1993 

Portage Transport of Toxophoric Agent, N-hydroxyalanine, through Oligopeptide Permease in Escherichia coli
Nam Joo Hong*, Yeong Taek Park
Di-and tri-peptides containing DL-N-hydroxyalanine were prepared. DL-N-Hydroxyalanine was linked, via its primary amino group, to the α-carbon of glycine residues in dipeptide synthon (L-alanyl(α -DL-N-hydroxyalanyl)DL-glycine) 5, and tripeptide synthon (L-alanyl-L-alanyl(α-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.
674 - 678
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