Intracellular glutathione concentrations are much higher than those in the blood, and glutathione-sensitive lovers are designed to take advantage of this gradient. Glutathione based junctions exploit REDOX reactions between mercaptan and disulfide to target this free mercaptan (glutathione) gradient between intracellular and extracellular space. Disulfide is relatively stable in circulation, but after internalization, free drugs are released by the reductive environment that exists in the cell. The stability of the disulfide bond in the cycle can be further enhanced by introducing methyl groups on both sides of the disulfide bond, thereby increasing steric hindrance and slowing cleavage rate at low free mercaptan concentrations. Steric hindrance disulfide bonds have been used in a number of clinical drug candidates, such as AVE9633 (anti-CD33 medendine conjugate), SAR3419 (anti-CD19 medendine conjugate), and IMGN901 (anti-CD56 medendine conjugate). 74 Erickson et al. The intracellular cleavage mechanism of disulfide junctions was investigated and a large number of lysine-bound disulfide drugs were found in the metabolites degraded by ADC, suggesting that the antibody undergoes proteolytic degradation and then releases the drug through glutathione reduction.

Glutathione, also known as GSH, is an endogenous component of cell metabolism and is a tripeptide composed of glycine, cysteine, and glutamate. It is usually present in the liver at a concentration of 10 mmol L-1. It is an integral part of the bioconversion of isobiomass to protect the body from reducing agents. Glutathione binding (facilitated by the glutathione transferase family) contributes to detoxification by binding electrophiles that may bind to proteins or nucleic acids, resulting in cell damage and genetic mutations. The existence of truly specific binding sites for GSH in the central nervous system has been reported, which meets the main requirement for treating GSH as a neurotransmitter, among other functions.

Glutathione is a tripeptide (gamma-glutamyl-cysteyl-glycine) in which cysteine can be in a reduced or oxidized glutathione state. Reduced glutathione either interacts with free radicals to form relatively unstable sulfhydryl radicals or directly inhibits lipid oxidation by providing an electron source, which allows glutathione peroxidase to enzymatically decompose hydrogen peroxide and lipid peroxides. Total glutathione concentrations in muscle foods range from 0.7 to 0.9 ug/kg. Seven healthy adults who took 3.0 glutathione orally did not increase plasma glutathione or cysteine concentrations after 270 minutes. Bioavailability of glutathione in rats is also reported to be low. Glutathione deficiency or low absorption rate may be due to the hydrolysis of tripeptides by gastrointestinal proteases.