ArticlePloS one2021
Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 13 citations in OpenAlex.
- Design and Synthesis of Phosphonoproline-Proline Bioisosteric Mimetics of Proline Dimers: Pseudopeptide Constructs as Potential Inhibitors of the Zn-Metalloprotease PPEP‑1 Associated withACS medicinal chemistry letters · 2026Article
- Repurposing azole antifungals as rapid bactericidal, membrane-disruptive therapeutics againstMicrobiology spectrum · 2026Article
- Coupling Far-Western Blotting with Peptide Microarrays Reveals Novel E-Cadherin Spore-Surface Ligands inJournal of proteome research · 2026Article
- Ionomycin Exhibits Potent and Selective Bactericidal Activity Against Clostridioides difficile Through Calcium-Dependent Membrane Disruption.MicrobiologyOpen · 2026Article
- Natural and synthetic antimicrobial peptides against anaerobic bacteria: A review of activities and mechanisms of action.Probiotics and antimicrobial proteins · 2026Review
- Unravelling three-way interactions betweenJournal of medical microbiology · 2025Review
- Potent Antimicrobial Activity ofAntibiotics (Basel, Switzerland) · 2025Article
- ApoE COG 133 mimetic peptide improves survival, infection burden, andExperimental biology and medicine (Maywood, N.J.) · 2025Article
- A rationally designed antimicrobial peptide from structural and functional insights ofMicrobiology spectrum · 2024Article
- The Effect of Antimicrobial Peptide (PA-13) onAntibiotics (Basel, Switzerland) · 2024Article
- Host-defense piscidin peptides as antibiotic adjuvants against Clostridioides difficile.PloS one · 2024Article
- Foodborne Clostridioides Species: Pathogenicity, Virulence and Biocontrol Options.Microorganisms · 2023Review
- New treatment approaches forGut microbesReview
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridioides difficile infection is the most common cause of nosocomial and antibiotic-associated diarrhea. C. difficile treatment is increasingly likely to fail, and the recurrence rate is high. Antimicrobial peptides are considered an alternative treatment for many infectious diseases, including those caused by antibiotic resistant bacteria. In the present study, we identified a CM peptide, a hybrid of cecropin A and melittin, and its derivative which possesses potent antimicrobial activity against C. difficile strain 630. CM peptide exhibited antibacterial activity with minimum inhibitory concentration of 3.906 μg/ml (2.21 μM). A modified derivative of CM, CM-A, exhibited even greater activity with a minimum inhibitory concentration of 1.953 μg/ml (1.06 μM) and a minimum bactericidal concentration of 7.8125 μg/ml (4.24 μM), which indicates that CM-A peptide is more efficient than its parent peptide. A fluorescence-activated cell sorter analysis revealed that the membrane of C. difficile 630 could be an important target for CM-A. This peptide induced high levels of cell depolarization and cell permeability on C. difficile cell membrane. Moreover, electron microscopy imaging showed that CM-A interferes with the C. difficile cell membrane. Hence, the antimicrobial peptide CM-A may represent a promising novel approach for the treatment of C. difficile 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.