Metal-binding and detoxification effect of synthetic oligopeptides containing three cysteinyl residues.
Metallothionein is a naturally occurring metal-binding protein with high cysteine content. Oligopeptides containing three cysteinyl residues and having amino acid sequences analogous to portions of this protein were synthesized by the solid-phase method. Strong affinity of the synthetic peptides to Cd2+ and Zn2+ was observed, and the dissociation constants of the peptide-metal complexes were 2-4 orders of magnitude lower than those of cysteine-metal and dithioerythritol-metal complexes. Effectiveness of detoxification of the peptides against Cd toxicity was demonstrated by the higher survival rates of mice treated with the peptides and by the neutralization of Cd toxicity by the peptides in tissue cultures.
D002413:Cations, Divalent / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000633:toxicity; D002478:Cells, Cultured / Q000187:drug effects; D003545:Cysteine; D008667:Metalloproteins / Q000378:metabolism; D008668:Metallothionein / Q000031:analogs & derivatives / Q000378:metabolism; D008670:Metals; D009842:Oligopeptides / Q000378:metabolism*; D013329:Structure-Activity Relationship
D002413:Cations, Divalent; D008667:Metalloproteins; D008670:Metals; D009842:Oligopeptides; D008668:Metallothionein; D003545:Cysteine