Glutathione is a tripeptide composed of amino acid residues of glutamate, cysteine, and glycine (γ-L-glutamyl-L-cysteinyl-glycine). It’s primarily synthesized in liver cells. This peptide is one of the most widespread intracellular peptides involved in amino acid transport across the cell membrane, and it plays a crucial role in oxidative-reductive and other processes within the cell. Despite mixed data about its effectiveness when introduced exogenously, glutathione remains a widely used peptide in sports nutrition products.
Glutathione is often included in the composition of multicomponent sports nutrition mixes, especially in strength sports. Studies have shown the effectiveness of such compositions (Hoffman J.R. et al., 2009; Jagim A.R. et al., 2016). However, as these mixes often contain other ergogenic nutrabolics like caffeine, BCAAs, creatine, and β-alanine, isolating the specific effect of glutathione is challenging.
Physical exertion reduces the levels of reduced glutathione and increases the oxidized form (Gambelunghe C. et al., 2001). A decrease in glutathione concentrations in blood plasma and tissues is noted with the increase in duration of workouts beyond a certain time (Lew H. et al., 1985; Pyke S. et al., 1986; Georgakouli K. et al., 2017), confirming the link between the glutathione system, aerobic energy metabolism, and muscle contraction process.
Significant advancements have been made in increasing glutathione’s bioavailability. A sublingual form of the tripeptide has been developed, with pharmacokinetic crossover studies conducted by B. Schmitt and colleagues (2015) on a group of patients with metabolic syndrome (n = 20, three weeks of intake and observation). The sublingual form of glutathione showed advantages over oral forms in terms of bioavailability and positive effects on adaptation to oxidative stress. However, studies in sports nutrition on this topic are yet to be conducted.