Comparison of the stability of glutathione and related synthetic tetrapeptides by HPLC and capillary electrophoresis.
Glutathione and related peptides are interesting targets as protectors of biological systems against an oxidative injury. Two novel glutathione analogues, UPF1 and UPF15, have been designed and synthesised. As a result of different reactions taking place, the thiol-containing compounds oxidise to disulfides. In this study, the stability of UPF1, UPF15 and glutathione in various solutions was investigated by using HPLC and CE. The results showed that UPF1 and UPF15 are powerful hydroxyl radical scavengers and their dimerisation process velocity is higher than that of glutathione.
Mahlapuu
Riina
R
Department of Biochemistry, Faculty of Medicine, University of Tartu; National and European Centre of Excellence of Molecular and Clinical Medicine, Ravila Str. 19, 50411 Tartu, Estonia. riina.mahlapuu@ut.ee
Vaher
Merike
M
Ehrlich
Kersti
K
Kaljurand
Mihkel
M
Soomets
Ursel
U
D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D004220:Disulfides / Q000737:chemistry; D004355:Drug Stability; D019075:Electrophoresis, Capillary / Q000379:methods*; D005978:Glutathione / Q000031:analogs & derivatives / Q000737:chemistry*; D017665:Hydroxyl Radical / Q000737:chemistry; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*
D004220:Disulfides; D009842:Oligopeptides; D017665:Hydroxyl Radical; D005978:Glutathione