Structure-function relationships in glutathione and its analogues.
The results are presented of measurements of protonation constants (potentiometry and NMR), UV spectroscopic properties and redox potentials of GSH and its five analogues, which are modified at the C-terminal glycine residue (gammaGlu-Cys-X, X = Gly, Gly-NH2, Gly-OEt, Ala, Glu, Ser). Strong linear correlations were found between various properties of the thiol and other functions of these peptides. These results allow discussion of the relationships between the structures and properties in glutathione and its analogues, and provide a novel chemical background for the issue of control of GSH reactivity.
Krezel
Artur
A
Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wrocław, Poland. arti@wcheto.chem.uni.wroc.pl
Bal
Wojciech
W
D004583:Electrons; D005978:Glutathione / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D011199:Potentiometry; D017434:Protein Structure, Tertiary; D011522:Protons; D013053:Spectrophotometry; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000737:chemistry; D014466:Ultraviolet Rays
D010455:Peptides; D011522:Protons; D013438:Sulfhydryl Compounds; D005978:Glutathione; D010100:Oxygen