ArticleACS omega2025
Cyclization of Two Antimicrobial Peptides Improves Their Activity.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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
14 citing papers in PubMed.
- Next-Generation Antimicrobial Peptides for Biofilm-Associated Infections: Engineering, Biomaterial Delivery and AI-Assisted Discovery.Antibiotics (Basel, Switzerland) · 2026Review
- Article
- Cyclic Peptides in Modern Drug Discovery: Trends and Therapeutic Directions.Journal of medicinal chemistry · 2026Review
- Identification and Optimization of a Truncated Hs-1-Derived Antimicrobial Peptide for Enhanced Broad-Spectrum Antiviral Activity.ChemMedChem · 2026Article
- Exploring the antibacterial potential of a designed peptide against Gardnerella vaginalis.Molecular biology reports · 2026Article
- Modular peptide nanofibres that self-assemble on bacterial membranes overcome antimicrobial resistance.Nature biomedical engineering · 2026Article
- Integrative Peptide Drug Development: Chemical Engineering, AI-Driven Design, and Cell-Penetrating Peptides.Pharmaceutics · 2026Review
- Structural Modification and Conjugation Strategies of Antimicrobial Peptides for Topical Anti-Infective Applications.Antibiotics (Basel, Switzerland) · 2026Review
- Artificial Intelligence-Driven Discovery and Optimization of Antimicrobial Peptides Targeting ESKAPE Pathogens and Multidrug-Resistant Fungi.Microorganisms · 2026Review
- Natural and Synthetic Peptides as Alternatives to Antibiotics in Intestinal Infections-A Review.Antibiotics (Basel, Switzerland) · 2026Review
- Impact of the Arrangement Modes of the Antimicrobial Motifs WWR-7 and its Analogs in CAMPs on Their Therapeutic Properties.Chemistry, an Asian journal · 2026Article
- Anti-SARS-CoV-2 VHH and C7C peptide fused with Angiopep-2 efficiently traverse blood-brain barrier model and neutralizes virus.Frontiers in microbiology · 2026Article
- Boosting AMPs' Power: From Structural Engineering to Nanotechnology-Based Delivery.Molecules (Basel, Switzerland) · 2025Review
- Antimicrobial Peptides in Wound Healing and Skin Regeneration: Dual Roles in Immunity and Microbial Defense.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
One promising strategy to combat worldwide antimicrobial resistance involves using cyclic peptides as antibacterial agents. Cyclization of peptides can confer several advantages, including enhanced stability to proteolysis, decreased toxicity and increased bactericidal efficacy. This paper examines two cyclic peptides CE-03 (12 AAs) and CE-05 (16 AAs) and evaluates their effectiveness in combating bacterial infections, their stability and toxicity. We compare them to their linear versions. Circular dichroism (CD) reveals that CE-03 and CE-05 both adopt random coil and β-sheet structures in lipid model membranes (LMMs) mimicking G(-) and G(+) bacteria, where they are both bactericidal. Using X-ray diffuse scattering (XDS), their effects on lipid model membranes show a deep penetration of both peptides into eukaryotic LMMs where they are nontoxic, while a headgroup location in bacterial LMMs correlates with bacterial killing. Neutron reflectometry (NR) confirms the AMP locations determined using XDS. Further, solution small-angle X-ray scattering demonstrates that both peptides induce vesicle fusion in bacterial LMMs without affecting eukaryotic LMMs. Proteolytic degradation studies show that both CE-05 and CE-03 do not lose activity when incubated with the elastase enzyme, while the helical E2-35 AMP becomes inactive upon proteolysis.
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.