Journal article
Cellular disulfide bond formation in bioactive peptides and proteins
NA Patil, J Tailhades, RA Hughes, F Separovic, JD Wade, MA Hossain
International Journal of Molecular Sciences | MDPI | Published : 2015
DOI: 10.3390/ijms16011791
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..
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Grants
Awarded by National Health and Medical Research Council
Funding Acknowledgements
This research was partly funded by NHMRC (Australia) project grant (1023321) and an ARC Linkage grant (LP120100654). The Victorian Government's Operational Infrastructure Support Program supported research at the FNI. Nitin A. Patil thanks the University of Melbourne for providing Melbourne International Research Scholarship.