Mthembu Sinenhlanhla N, Sharma Anamika, Albericio Fernando, de la Torre Beatriz G
Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban, 4001, South Africa.
KRISP, School of Laboratory of Medicine and Medical Sciences College of Health Sciences, University of KwaZulu-Natal Westville, Durban, 4001, South Africa.
Chembiochem. 2020 Jul 16;21(14):1947-1954. doi: 10.1002/cbic.202000092. Epub 2020 Apr 30.
Cysteine is present in a large number of natural and synthetic (bio)molecules. Although the thiol side chain of Cys can be in a free form, in most cases it forms a disulfide bond either with a second Cys (bridge) or with another thiol, as in the case of protecting groups. Efficient reduction of these disulfide bridges is a requirement for many applications of Cys-containing molecules in the fields of chemistry and biochemistry. Here we review reducing methods for disulfide bonds, taking into consideration the solubility of the substrates when selecting the appropriate reducing reagent.
半胱氨酸存在于大量天然和合成（生物）分子中。虽然半胱氨酸的硫醇侧链可以呈游离形式，但在大多数情况下，它会与第二个半胱氨酸形成二硫键（桥），或者与另一个硫醇形成二硫键，如保护基团的情况。有效还原这些二硫键桥是含半胱氨酸分子在化学和生物化学领域许多应用的必要条件。在此，我们在选择合适的还原剂时考虑底物的溶解度，综述二硫键的还原方法。
