ArticleFrontiers in microbiology2025
Development of lysine-branched dendrimeric antimicrobial peptides targeting ESKAPE pathogens: broad-spectrum activity, biofilm eradication, and endotoxin neutralization.
Article in Frontiers in microbiology, 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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Abstract
Antimicrobial resistance (AMR) represents a pressing global health challenge, driving the urgent need for novel therapeutic agents with improved stability and selectivity. In this study, we present the rational design and synthesis of lysine-branched dendrimeric antimicrobial peptides (AMPs) based on short arginine/tryptophan-rich motifs (Du-6 and Lf-6), yielding dimeric and tetrameric architectures. Physicochemical analyses revealed a systematic increase in net charge and hydrophobicity with higher degrees of branching. Comparative biological evaluations demonstrated that dimeric peptides (di-Du-6 and di-Lf-6) achieved optimal broad-spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria, including multidrug-resistant ESKAPE pathogens. These dimers maintained low hemolytic activity and exhibited therapeutic indices of up to 40. In contrast, despite their elevated charge density and tryptophan content, tetrameric peptides showed increased cytotoxicity, likely due to deeper membrane penetration into eukaryotic cells, thereby compromising selectivity. To overcome proteolytic degradation, D-enantiomeric dimers [(di-Du-6)
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