Multiple pairs of disulfide bonds

Disulfide bonds are an integral part of the three-dimensional structure of many proteins. We can find these covalent bonds in almost all extracellular peptide and protein molecules. A disulfide bond is formed when the sulfur atom of one cysteine forms a covalent single bond with the sulfur atom of another cysteine located at a different location in the protein. These bonds help stabilize proteins, especially those secreted from cells.

If the polypeptide contains only 1 pair Cys, The formation of that disulfide bond is simple. Peptides are synthesized in solid phase or liquid phase and then pH8-9 oxidation is carried out in the solution.

When two or more pairs of disulfide bonds need to be formed, the synthesis process is relatively complicated. Although the formation of disulfide bonds is usually accomplished at the end of the synthetic scheme, it is sometimes advantageous to introduce preformed disulfides to conjugate or extend the peptide chain. Commonly used sulfhydryl protecting groups are trt, Acm, Mmt, tBu, Bzl, Mob, Tmob and other groups. We list two types respectively with 2- Cl resin and Rink The formation route of multiple pairs of disulfide bonds on polypeptides synthesized using resin as a carrier: