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

doi:10.3390/ijms16011791

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 journal › Review Article › Research › peer-review

59 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1791-1805
Number of pages	15
Journal	International Journal of Molecular Sciences
Volume	16
Issue number	1
DOIs	https://doi.org/10.3390/ijms16011791
Publication status	Published - 14 Jan 2015
Externally published	Yes

Keywords

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

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AU - Patil, Nitin A.

AU - Tailhades, Julien

AU - Hughes, Richard Anthony

AU - Separovic, Frances

AU - Wade, John D.

AU - Hossain, Mohammed Akhter

PY - 2015/1/14

Y1 - 2015/1/14

N2 - 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.

AB - 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.

KW - Bioactive peptides

KW - Disulfide bonds

KW - Oxidative folding

KW - Peptide and protein folding

KW - Recombinant technology

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M3 - Review Article

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AN - SCOPUS:84921300490

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JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

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Cellular disulfide bond formation in bioactive peptides and proteins

Abstract

Keywords

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