Pyrrhocoricin | |||||||
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![]() The firebug Pyrrhocoris apterus | |||||||
Identifiers | |||||||
Symbol | ? | ||||||
CAS number | |||||||
PDB | 5FDV | ||||||
UniProt | P37362 | ||||||
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Pyrrhocoricin is a 20-residue long antimicrobial peptide of the firebug Pyrrhocoris apterus. [1]
Pyrrhocoricin is primarily active against Gram-negative bacteria. The peptide is proline-rich with proline-arginine repeats, as well a critical threonine residue, which is required for activity through O-glycosylation. Like the antimicrobial peptides drosocin and abaecin, pyrrhocoricin binds to the bacterial protein DnaK, inhibiting cell machinery and replication. [2] Only the L-enantiomer of pyrrhocoricin is active against bacteria. [3] The action of pyrrhocoricin-like peptides is potentiated by the presence of pore-forming peptides, which facilitates the entry of pyrrhocoricin-like peptides into the bacterial cell. [4] Proline-rich peptides like Pyrrhocoricin can also bind to microbe ribosomes, preventing protein translation. [5] In the absence of pore-forming peptides, pyrrhocoricin is taken into the bacteria by the action of bacterial uptake permeases. [6]
Pyrrhocoricin | |||||||
---|---|---|---|---|---|---|---|
![]() The firebug Pyrrhocoris apterus | |||||||
Identifiers | |||||||
Symbol | ? | ||||||
CAS number | |||||||
PDB | 5FDV | ||||||
UniProt | P37362 | ||||||
|
Pyrrhocoricin is a 20-residue long antimicrobial peptide of the firebug Pyrrhocoris apterus. [1]
Pyrrhocoricin is primarily active against Gram-negative bacteria. The peptide is proline-rich with proline-arginine repeats, as well a critical threonine residue, which is required for activity through O-glycosylation. Like the antimicrobial peptides drosocin and abaecin, pyrrhocoricin binds to the bacterial protein DnaK, inhibiting cell machinery and replication. [2] Only the L-enantiomer of pyrrhocoricin is active against bacteria. [3] The action of pyrrhocoricin-like peptides is potentiated by the presence of pore-forming peptides, which facilitates the entry of pyrrhocoricin-like peptides into the bacterial cell. [4] Proline-rich peptides like Pyrrhocoricin can also bind to microbe ribosomes, preventing protein translation. [5] In the absence of pore-forming peptides, pyrrhocoricin is taken into the bacteria by the action of bacterial uptake permeases. [6]