Fig. 2: Structure optimization of BNP37 analogs leading to the discovery of paenimicin. | Nature Communications

Fig. 2: Structure optimization of BNP37 analogs leading to the discovery of paenimicin.

From: A broad-spectrum antibiotic targets multiple-drug-resistant bacteria with dual binding targets and no detectable resistance

Fig. 2

a Diagrams of five peptide topologies predicted to be arisen from BNP37 BGC, along with their antimicrobial activity and serum binding efficacy against ESKAPE pathogens of all the peptides. (E. faecium BNCC 186301, S. aureus BNCC 186335, K. pneumoniae BNCC 186113, A. baumannii BNCC 194496, P. aeruginosa BNCC 186070, E. cloacae BNCC 185028). b The BGC of BNP37. 10-signature code sequences were used to predict each adenylation (A) domain, with the prediction accuracy was deemed reliable when it reached 80%. c Fold changes in MIC following 2,4-Diaminobutyric Acid (Dab) screening. Specifically, all non-Dab positions were replaced with Dab respectively, MIC values against methicillin-resistant S. aureus (MRSA, S. aureus ATCC BAA44) and carbapenems-resistant A. baumannii (CRAB, A. baumannii ATCC BAA1605) with 10% serum were evaluated. N/A: not applicable. d Structure of paenimicin.

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