RTI uses cookies to offer you the best experience online. By clicking “accept” on this website, you opt in and you agree to the use of cookies. If you would like to know more about how RTI uses cookies and how to manage them please view our Privacy Policy here. You can “opt out” or change your mind by visiting: http://optout.aboutads.info/. Click “accept” to agree.
Cellular disulfide bond formation in bioactive peptides and proteins
Patil, N. A., Tailhades, J., Hughes, R. A., Separovic, F., Wade, J. D., & Hossain, M. A. (2015). Cellular disulfide bond formation in bioactive peptides and proteins. International Journal of Molecular Sciences, 16(1), 1791-1805. https://doi.org/10.3390/ijms16011791
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.
RTI shares its evidence-based research - through peer-reviewed publications and media - to ensure that it is accessible for others to build on, in line with our mission and scientific standards.
