Glutathione is a tripeptide, made up of the three amino acids cysteine, glutamic acid and glycine. It has gained significant popularity among nutritionists, as it is one of the most prevalent anti-oxidants in the body.

Anti-oxidants have gained fame as one of the most useful additions to one’s diet, as they are responsible for preventing the damage to cells by de-stabilising molecules, such as reactive oxygen species (ROS). These species can be produced by a number of cellular sources and are a normal by-product of aerobic respiration. Environmental stimuli, such as ionizing radiation, can also greatly increase ROS production.

The effects of increased ROS production, which means cells experience ‘oxidative stress’, can be extremely serious. ROS can damage DNA, oxidize lipids and fatty acids, oxidize the amino acids that make up proteins and inactivate key enzymes, due to the oxidization of co-factors. These effects can severely hamper the activity of a cell and can, in some instances lead to its destruction. For example, damage to the mitochondria can lead to the leakage of molecules that bring about the process of apoptosis, the programmed death of a cell, into the cytoplasm.

Anti-oxidants prevent the action of these ROS by removing their extreme reactivity. In order to counteract ROS, glutathione has to exist in its reduced state (GSH). The thiol group (highlighted in blue in the image below) donates either a hydrogen ion or an electron to ROS. In donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form the innert glutathione disulfide.

Glutathione is becoming more popular both nutritionally and in the research of therapeutics, as oxygen free radicals, inhibited by glutathione, are linked to the DNA and protein damage associated with the process of ageing and the development of cancer.

‘Til next time…


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