Ferrocene labelings as inhibitors and dual electrochemical sensors of human glutathione S-transferase P1-1.
The inhibitory and sensor properties of two ferrocene conjugates, in which the ferrocene and glutathione are linked through a spacer arm of different length and chemical structure, on human Pi glutathione S-transferase, were examined by activity assays, ITC, fluorescence spectroscopy and voltammetry. Such ferrocene conjugates are strong competitive inhibitors of this enzyme with an enhanced binding affinity, the one bearing the longest spacer arm being the most potent inhibitor. Voltammetric measurements showed a strong decrease of the peak current intensity and an increase of the oxidation potential upon binding of ferrocene-glutathione conjugates to GST P1-1 showing that both conjugates can be used as dual electrochemical sensors for GST P1-1.
Department of Chemistry and Physics, University of Almería, Crta.de Sacramento s/n, 04120 Almería, Spain.
Manuel C
MC
Martos-Maldonado
Indalecio
I
Quesada-Soriano
Federico
F
García-Maroto
Antonio
A
Vargas-Berenguel
Luís
L
García-Fuentes
D002151:Calorimetry; D055664:Electrochemical Techniques; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry*; D005296:Ferrous Compounds / Q000737:chemistry*; D005978:Glutathione / Q000737:chemistry; D051549:Glutathione S-Transferase pi / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D000075163:Metallocenes; D010084:Oxidation-Reduction; D011485:Protein Binding; D013816:Thermodynamics
D004791:Enzyme Inhibitors; D005296:Ferrous Compounds; D000075163:Metallocenes; D051549:Glutathione S-Transferase pi; D005978:Glutathione; C004998:ferrocene