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Cracking the Code of the Disulfide bond

  • 1 min read

Glutathione is literally in every cell of the human body. Glutathione was discovered in 1888 by J. De Rey-Pailhide. However, its bodily replenishment was often hindered by synthesis complexities and by the inability of the rate-limiting L-Cysteine to arrive safely into cells to participate in the synthesis of Glutathione. As it is a true-tide, Glutathione is composed of three amino acids: L-Cysteine, a Glutamate source, and Glycine. 

For years, many scientists thought that the disulfide bond of L-Cysteine was so strong, that once it is locked, in an oxidized state, that this amino acid was being prepared for excretion. 

In a lab at Harvard, it was discovered that the disulfide bond is physiologically reversible under substrate-specific enzymes that exist in the cytosol of each cell. They also discovered:

  • That the oxidized state can be a carrier and protector of L-Cysteines. Although an oxidized molecule itself, it saved the L-Cysteine from irreversible oxidation to the compounds: Sulfuric acid, Sulfinic acid and Sulfonic acid and their excretion.
  • The disulfide bond is also capable of holding in reserve and preserving additional molecules of L-Cysteine via an electron transfer coupling mechanism.
  • As a biomarker of Oxidative Stress, the disulfide bond can also signal the genome for genomic intervention commensurate with the immunological challenge being confronted.

By understanding the reverse engineering the process of the Cystine and Cysteine molecules, what before was known as a pleiotropic paradox, was now solved. In biochemistry, this is called the precursor method: a chemical compound preceding another in a metabolic pathway. This discovery is what also makes IF200™ patented.