Abstract
By using the chain to chain mode of cyclization the title glutathione analogue (4), containing the 11-membered disulfide ring replacing the native -Cys-Gly fragment, has been synthesized and characterized together with its reduced dithiol form gamma-Glu-Cys-Asp-Cys (5). The activity of (4) with gamma-glutamyl-transferase and glutathione reductase has been evaluated and compared with those of the two conformationally restricted glutathione analogues (2) and (3) previously reported.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cattle
-
Disulfides / chemistry*
-
Enzyme Inhibitors / chemical synthesis*
-
Enzyme Inhibitors / chemistry
-
Enzyme Inhibitors / pharmacology
-
Glutathione / analogs & derivatives*
-
Glutathione / chemical synthesis
-
Glutathione / pharmacology
-
Glutathione Reductase / antagonists & inhibitors
-
Kidney / enzymology
-
Oligopeptides / chemical synthesis*
-
Oligopeptides / chemistry
-
Oligopeptides / pharmacology
-
Saccharomyces cerevisiae / enzymology
-
Structure-Activity Relationship
-
Swine
-
gamma-Glutamyltransferase / antagonists & inhibitors
Substances
-
Disulfides
-
Enzyme Inhibitors
-
Oligopeptides
-
gamma-glutamyl-cysteinyl-aspartyl-cysteine
-
Glutathione Reductase
-
gamma-Glutamyltransferase
-
Glutathione