ArticleScientific reports2017
Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 77 citations in OpenAlex.
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- Time-resolved phenotyping at subcellular resolution reveals shared principles and key trade-offs across antimicrobial peptide activities.bioRxiv : the preprint server for biology · 2026Article
- Antimicrobial peptoids pass rapidly through bacterial membranes and flocculate ribosomes and DNA: A single-cell fluorescence study.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- SMAP29: an antibacterial peptide that possesses anti-inflammatory and fast bactericidal actions against colistin-resistant gram-negative bacteria.Microbiology spectrum · 2026Article
- Peptoid-based antimicrobial strategies against polymyxin-resistant Gram-negative bacteria.Journal of applied microbiology · 2026Article
- The dysregulation of innate immunity by Porphyromonas gingivalis in the etiology of Alzheimer's disease.Journal of internal medicine · 2026Review
- Proteasome Fine-Tunes the Generation of Antimicrobial Peptides.Current drug targets · 2026Review
- Extended-Spectrum β-Lactamase-ProducingAntibiotics (Basel, Switzerland) · 2025Review
- Antiparasitic effect of peptoids againstMicrobiology (Reading, England) · 2025Article
- Synthetic host defense peptide inhibits SARS-CoV-2 replicationAntimicrobial agents and chemotherapy · 2025Article
- Structural Optimization of Antifungal Peptoids targetingACS medicinal chemistry letters · 2025Article
- Antimicrobial Peptide-Peptoid Macrocycles from the Polymyxin B2 Chemical Space.Angewandte Chemie (International ed. in English) · 2025Article
- A biofilm-targeting lipo-peptoid to treatBiofilm · 2025Article
- Antimicrobial activity of peptoids against Metallo-β-lactamase-producing Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and other WHO priority pathogens, including Candida auris.Journal of applied microbiology · 2025Article
- Article
- Stereorandomized Oncocins with Preserved Ribosome Binding and Antibacterial Activity.Journal of medicinal chemistry · 2024Article
- Peptide-mimetic treatment of Pseudomonas aeruginosa in a mouse model of respiratory infection.Communications biology · 2024Article
- Deciphering the Intracellular Action of the Antimicrobial Peptide A11 via an In-Depth Analysis of Its Effect on the Global Proteome ofACS infectious diseases · 2024Article
- Between good and evil: Complexation of the human cathelicidin LL-37 with nucleic acids.Biophysical journal · 2024Review
- Peptides with Antimicrobial Activity in the Saliva of the Malaria VectorInternational journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Many organisms rely on antimicrobial peptides (AMPs) as a first line of defense against pathogens. In general, most AMPs are thought to kill bacteria by binding to and disrupting cell membranes. However, certain AMPs instead appear to inhibit biomacromolecule synthesis, while causing less membrane damage. Despite an unclear understanding of mechanism(s), there is considerable interest in mimicking AMPs with stable, synthetic molecules. Antimicrobial N-substituted glycine (peptoid) oligomers ("ampetoids") are structural, functional and mechanistic analogs of helical, cationic AMPs, which offer broad-spectrum antibacterial activity and better therapeutic potential than peptides. Here, we show through quantitative studies of membrane permeabilization, electron microscopy, and soft X-ray tomography that both AMPs and ampetoids trigger extensive and rapid non-specific aggregation of intracellular biomacromolecules that correlates with microbial death. We present data demonstrating that ampetoids are "fast killers", which rapidly aggregate bacterial ribosomes in vitro and in vivo. We suggest intracellular biomass flocculation is a key mechanism of killing for cationic, amphipathic AMPs, which may explain why most AMPs require micromolar concentrations for activity, show significant selectivity for killing bacteria over mammalian cells, and finally, why development of resistance to AMPs is less prevalent than developed resistance to conventional antibiotics.
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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.