Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins |
| |
| Authors: | Nitin A. Patil Julien Tailhades Richard Anthony Hughes Frances Separovic John D. Wade Mohammed Akhter Hossain |
| |
| Affiliation: | 1.Florey Institute of Neuroscience and Mental Health, the University of Melbourne, Victoria 3010, Australia; E-Mails: (N.A.P.); (J.T.); (J.D.W.);2.School of Chemistry, the University of Melbourne, Victoria 3010, Australia; E-Mail: ;3.Department of Pharmacology and Therapeutics, the University of Melbourne, Victoria 3010, Australia; E-Mail: ;4.Florey Departments of Neuroscience and Mental Health, the University of Melbourne, Victoria 3010, Australia |
| |
| Abstract: | Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of enzymes—a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor—that function inside the cell dictates the formation and maintenance of disulfide bonds. The main pathways that catalyze disulfide bond formation in peptides and proteins in prokaryotes and eukaryotes are remarkably similar and share several mechanistic features. This review summarizes the formation of disulfide bonds in peptides and proteins by cellular and recombinant machinery. |
| |
| Keywords: | bioactive peptides disulfide bonds peptide and protein folding oxidative folding recombinant technology |
|
|
