Unexpected diselenide metathesis in selenocysteine-substituted biologically active peptides

Substitution of disulfide bonds with a diselenide bonds in peptides and proteins is an often-used strategy to increase the stability of naturally occurring peptides and proteins. In this paper, diselenide metathesis between model diselenide dimer peptides, as well as that in diselenide(s)-substitute...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2024-07, Vol.22 (3), p.618-6114
Main Authors: He, Ying, Takei, Toshiki, Moroder, Luis, Hojo, Hironobu
Format: Article
Language:English
Subjects:
Biological activity
Bonding agents
Disulfide bonds
Metathesis
Molecular structure
Organoselenium Compounds - chemical synthesis
Organoselenium Compounds - chemistry
Peptides
Peptides - chemical synthesis
Peptides - chemistry
Protein structure
Proteins
Reducing agents
Selenocysteine
Selenocysteine - chemistry
Substitution reactions
Tertiary structure
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Summary:Substitution of disulfide bonds with a diselenide bonds in peptides and proteins is an often-used strategy to increase the stability of naturally occurring peptides and proteins. In this paper, diselenide metathesis between model diselenide dimer peptides, as well as that in diselenide(s)-substituted biologically active peptides, were analyzed. Surprisingly, depending on the tertiary structure of the peptides, we observed that the metathesis reaction occurs under physiological conditions even in the absence of reducing agents, light and heating. Substitution of disulfide bonds with a diselenide bonds in peptides and proteins is an often-used strategy to increase the stability of naturally occurring peptides and proteins.
ISSN:1477-0520
1477-0539
1477-0539
DOI:10.1039/d4ob00921e