Cellular disulfide bond formation in bioactive peptides and proteins

Nitin A. Patil, Julien Tailhades, Richard Anthony Hughes, Frances Separovic, John D. Wade, Mohammed Akhter Hossain

Research output: Contribution to journalReview ArticleResearchpeer-review

44 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1791-1805
Number of pages15
JournalInternational Journal of Molecular Sciences
Issue number1
Publication statusPublished - 14 Jan 2015
Externally publishedYes


  • Bioactive peptides
  • Disulfide bonds
  • Oxidative folding
  • Peptide and protein folding
  • Recombinant technology

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