Cellular disulfide bond formation in bioactive peptides and proteins
Nitin A Patil1, Julien Tailhades2, Richard Anthony Hughes3
1Florey Institute of Neuroscience and Mental Health, the University of Melbourne, Victoria 3010, Australia. fs@unimelb.edu.au.
International Journal of Molecular Sciences
|January 17, 2015
Summary
Cellular machinery forms disulfide bonds crucial for bioactive peptide structure and function. This review details the enzymes and pathways involved in disulfide bond generation and maintenance in both prokaryotes and eukaryotes.
Area of Science:
- Biochemistry
- Molecular Biology
- Peptide Chemistry
Background:
- Bioactive peptides are vital for metabolic regulation and therapeutic applications.
- Disulfide bonds are essential for the structural integrity, function, and stability of many peptides.
- Cellular enzymes orchestrate the formation and maintenance of these critical disulfide bonds.
Purpose of the Study:
- To review the mechanisms of disulfide bond formation in peptides and proteins.
- To summarize the cellular and recombinant machinery involved in disulfide bond generation.
- To highlight the similarities in disulfide bond formation pathways across prokaryotes and eukaryotes.
Main Methods:
- Literature review of enzymatic pathways for disulfide bond formation.
- Analysis of cellular and recombinant systems for peptide modification.
- Comparative study of disulfide bond formation in prokaryotic and eukaryotic systems.
Main Results:
- A systematic enzymatic network, including disulfide bond generating and donor enzymes with redox cofactors, governs disulfide bond formation.
- Cellular machinery for disulfide bond formation in prokaryotes and eukaryotes shares conserved mechanistic features.
- Both endogenous cellular processes and recombinant systems can be utilized for disulfide bond generation.
Conclusions:
- Understanding disulfide bond formation is key to peptide-based therapeutics.
- Cellular enzymatic pathways provide a conserved model for peptide and protein disulfide bond generation.
- The review consolidates knowledge on disulfide bond formation by both natural and engineered biological systems.
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