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Short Proline‐Rich Antimicrobial Peptides Inhibit Either the Bacterial 70S Ribosome or the Assembly of its Large 50S Subunit
Author(s) -
Krizsan Andor,
Prahl Caroline,
Goldbach Tina,
Knappe Daniel,
Hoffmann Ralf
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500375
Subject(s) - antimicrobial peptides , protein subunit , ribosome , chemistry , proline , peptide , antibacterial peptide , antimicrobial , biochemistry , translation (biology) , bacteria , biology , amino acid , rna , genetics , antibacterial activity , messenger rna , gene , organic chemistry
Short proline‐rich antimicrobial peptides (PrAMPs) are a promising class of antibiotics that use novel mechanisms, thus offering the potential to overcome the health threat of multiresistant pathogens. The peptides bind to the bacterial 70S ribosome and can inhibit protein translation. We report that PrAMPs can be divided into two classes, with each class binding to a different site, and thus use different lethal mechanisms. Oncocin‐type peptides inhibit protein translation in Escherichia coli by binding to the exit tunnel of the 70S ribosome with half maximal inhibitory concentrations (IC 50 values) of around 2 to 6 μmol L −1 , whereas apidaecin‐type peptides block the assembly of the large (50S) subunit of the ribosome, resulting in similar IC 50 values. The revealed mechanisms should allow the design of new antibiotics to overcome current bacterial resistance mechanisms.