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Api88 is an antimicrobial peptide (AMP) active against multiple-drug-resistant (MDR) bacterial pathogens It exhibits efficiency against Gram-negative pathogens systemically and kills E coli directly
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Api88 is a novel antibacterial designer peptide to treat . . .
The lead compound Api88 enters bacteria without lytic effects at the membrane and inhibits chaperone DnaK at the substrate binding domain with a K (D) of 5 μmol L The Api88-DnaK crystal structure revealed that Api88 binds with a seven residue long sequence (PVYIPRP), in two different modes
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Here we investigate how different metal ion environments (Na+, Mg2+, Ca2+) affect antimicrobial activity of PrAMPs derived from apidaecin 1b (Api88, Api137) and Oncopeltus antibacterial peptide 4 (Onc72, Onc112) against Pseudomonas aeruginosa and Escherichia coli
Multimodal binding and inhibition of bacterial ribosomes by . . .
Api88, a C-terminally amidated (-CONH 2) analog of Api137 (-COOH), binds to the same sites, occupies a third binding pocket and interferes with the translation process presumably without RF-trapping
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