AI Article Synopsis
- - Proline-rich antimicrobial peptides (PrAMPs) are being developed as potential treatments for infections caused by Gram-negative bacteria, with examples including apidaecins and oncocins.
- - These peptides kill bacteria by targeting specific cellular components, primarily by binding to the 70S ribosome, without damaging the bacterial cell membrane.
- - Apidaecins and oncocins exhibit strong binding to the ribosome, and oncocins are particularly effective at inhibiting protein synthesis, while the chaperone protein DnaK is not the main target of these peptides.
Article Abstract
Proline-rich antimicrobial peptides (PrAMPs) have been investigated and optimized by several research groups and companies as promising lead compounds to treat systemic infections caused by Gram-negative bacteria. PrAMPs, such as apidaecins and oncocins, enter the bacteria and kill them apparently through inhibition of specific targets without a lytic effect on the membranes. Both apidaecins and oncocins were shown to bind with nanomolar dissociation constants to the 70S ribosome. In apidaecins, at least the two C-terminal residues (Arg17 and Leu18) interact strongly with the 70S ribosome, whereas residues Lys3, Tyr6, Leu7, and Arg11 are the major interaction sites in oncocins. Oncocins inhibited protein biosynthesis very efficiently in vitro with half maximal inhibitory concentrations (IC50 values) of 150 to 240 nmol L(-1). The chaperone DnaK is most likely not the main target of PrAMPs but it binds them with lower affinity.
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| http://dx.doi.org/10.1002/anie.201407145 | DOI Listing |
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