ArticleProbiotics and antimicrobial proteins2025
Segment-Based Peptide Design Reveals the Importance of N-Terminal High Cationicity for Antimicrobial Activity Against Gram-Negative Pathogens.
Article in Probiotics and antimicrobial proteins, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Broad-Spectrum Gramicidin S Derivatives with Potent Activity Against Multidrug-Resistant Gram-Negative ESKAPE Pathogens.Antibiotics (Basel, Switzerland) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Host defense antimicrobial peptides (AMPs) are recognized candidates to develop a new generation of peptide antibiotics. While high hydrophobicity can be deployed in peptides for eliminating Gram-positive bacteria, high cationicity is usually observed in AMPs against Gram-negative pathogen. This study investigates how the sequence distribution of basic amino acids affects peptide activity. For this purpose, we utilized human cathelicidin LL-37 as a template and designed four highly selective ultrashort peptides with similar length, net charge, and hydrophobic content. LL-10 + , RK-9 + , KR-8 + , and RIK-10 + showed similar activity against methicillin-resistant Staphylococcus aureus in vitro and comparable antibiofilm efficacy in a murine wound model. However, these peptides showed clear activity differences against Gram-negative pathogens with RIK-10 + (i.e., LL-37mini2) being the strongest and LL-10 + the weakest. To understand this activity difference, we characterized peptide toxicity; the effects of salts, pH, and serum on peptide activity; and the mechanism of action and determined the membrane-bound helical structure for RIK-10 + by two-dimensional NMR spectroscopy. By writing an R program, we generated charge density plots for these peptides and uncovered the importance of the N-terminal high-density basic charges for antimicrobial potency. To validate this finding, we reversed the sequences of two peptides. Interestingly, sequence reversal weakened the activity of RIK-10 + but increased the activity of LL-10 + especially against Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii. Those more active peptides with high cationicity at the N-terminus are also more hydrophobic based on HPLC retention times. A database search found numerous natural sequences that arrange basic amino acids primarily at the N-terminus. Combined, this study not only obtained novel peptide leads but also discovered one useful strategy for designing novel antimicrobials to control drug-resistant Gram-negative pathogens.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.