ArticleSmall (Weinheim an der Bergstrasse, Germany)2025
A Self-Assembling Peptide with Nanoparticle-to-Fibril Transformation Exhibits Multimodal Antimicrobial Activity through Membrane Disruption and Quorum-Sensing Inhibition.
Article in Small (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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
2 citing papers in PubMed.
- Antimicrobial Peptide Nanoassemblies: Design, Response Mechanisms, and Biomedical Applications.Molecules (Basel, Switzerland) · 2026Review
- A Self-Assembling Peptide with Nanoparticle-to-Fibril Transformation Exhibits Multimodal Antimicrobial Activity through Membrane Disruption and Quorum-Sensing Inhibition.Small (Weinheim an der Bergstrasse, Germany) · 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
11 authors.
Funding
Abstract
Quorum sensing (QS) plays a crucial role in biofilm formation, virulence, and antibiotic resistance, making it an attractive target for combating multidrug-resistant pathogens. Here, self-assembling peptides are designed by incorporating amphiphilic monomers with distinct hydrophobic and hydrophilic termini to achieve optimal self-assembly dynamics and interaction with bacterial membranes. The lead peptide, SAP2-PEG, spontaneously forms nanoparticles that transform into fibrillar networks under membrane-mimicking conditions. The peptide exhibits potent antimicrobial activity against critical nosocomial pathogens at low micromolar concentrations and disrupts both pre-formed and nascent polymicrobial biofilms. Mechanistically, SAP2-PEG disrupts bacterial membranes while simultaneously inhibiting QS by downregulating key genes, including the las and rh1 systems in Pseudomonas aeruginosa, and the agr system components in Staphylococcus aureus, as validated through transcriptome analysis. Notably, the peptide showed effectiveness against polymicrobial biofilms in both wound and catheter-associated infections. In vivo, it significantly reduced P. aeruginosa lung and S. aureus systemic infection. These findings establish SAP2-PEG as a promising therapeutic candidate that combines direct antimicrobial action with QS disruption for combating biofilm-associated infections.
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.