Cystine

Cystine is the amino acid with the formula (SCH₂CH(NH₂)CO₂H)₂. It is a white solid that is slightly soluble in water. Each molecule of cystine is made from two molecules of cysteine, another sulfur-containing amino acid that, as its name suggests, is very similar to cystine, with which it can be interconverted. It serves two biological functions, a site of redox reactions and a mechanical linkage that allows proteins to retain their 3-dimensional structure. It is a nonessential amino acid, which means that the human body can synthesize it.

Formation and reactions

It is common in many foods such as eggs, meat, dairy products, and whole grains as well as skin, horns and hair. It was not recognized as being derived of proteins until it was isolated from the horn of a cow in 1899. Human hair and skin contain approximately 10–14% cystine by mass. It was discovered in 1810 by William Hyde Wollaston.

Redox

It is formed from the oxidation of two cysteine molecules, via the formation of a disulfide bond. In cell biology, cystine (found in proteins) can only exist in non-reductive (oxidative) organelles, such as the secretory pathway (ER, Golgi, Lysosomes, Vesicles and ECM). Meaning that in reductive conditions (Cytoplasm, Nucleus, etc.) cysteine is favorably found. The disulfide link is readily reduced to give the corresponding thiol cysteine. Typical thiols for this reaction are mercaptoethanol and dithiothreitol: