ArticleACS omega2025
Expanding the Range of Darobactin Derivatives by Amber Stop Codon Suppression To Introduce Non-canonical Amino Acids.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
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Abstract
The ribosomally synthesized and post-translationally modified peptide (RiPP) darobactin A is a promising new antibiotic candidate with anti-Gram-negative activity inflicted by the inhibition of the novel target BamA. Genome mining revealed many putative darobactin producer strains, but a limited number of compound modification options. In this study, the amber stop codon suppression technique was used to integrate non-canonical amino acids into the bicyclic heptapeptide, creating new darobactin derivatives. The C-terminal phenylalanine was replaced by non-canonical phenylalanine derivatives with different substituents. Darobactin A F7F, featuring a fluorine atom in the para position of the C-terminal phenylalanine, was purified to enable structure validation by NMR. Activity assays revealed antimicrobial potency against selected Gram-negative strains comparable to darobactin A.
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