ABSTRACT
Oxidative stress is to upregulate the pentose phosphate pathway (PPP). The PPP consists of two functional branches, glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconaste dehydrogenase (6PGD). Glutathione reductase (GR) has a significant role in catalyzing an oxidized glutathione form into a reduced form. The purpose of this study is to investigate the effects of brimonidine and proparacaine on the activity of 6PGD, G6PD, and GR enzymes purified from human erythrocytes. Brimonidine displayed considerable inhibition profile against G6PD with IC50 value and KI constant of 29.93 ± 3.56 and 48.46 ± 0.66 µM, respectively. On the other hand, proparacaine had no inhibitory effect against G6PD. KI values were found to be 66.06 ± 0.78 and 811.50 ± 11.13 µM for brimonidine and proparacaine, respectively, for 6PGD. KI values were found to be 144.10 ± 2.01 and 1,654.00 ± 26.29 µM for brimonidine and proparacaine, respectively, for GR. Herein, also in silico molecular docking studies were performed between drugs and enzymes.
