ArticleBMC microbiology2025
Novel antibacterial peptide HfAMP against methicillin-resistant Staphylococcus aureus.
Article in BMC microbiology, 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
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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
2 citing papers in PubMed.
- Integrated proteomics, molecular dynamics, andRSC advances · 2026Article
- A comprehensive review of emerging therapeutic strategies against methicillin-resistantFrontiers in microbiology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
objectivesThe urgent development of novel antibacterial agents to combat antibiotic-resistant Staphylococcus aureus is imperative. Antimicrobial peptides are considered promising alternatives to traditional antibiotics for addressing this pressing issue. This study investigates the antibacterial activities and potential mechanisms of the peptide HfAMP against methicillin-resistant S. aureus (MRSA).
methodsThe antibacterial activity of HfAMP against MRSA was evaluated using the broth microdilution method, growth curve, and time-kill assay. Its potential mechanism of action was investigated through propidium iodide, laurdan, DiSC
resultsThe results demonstrate that HfAMP exhibits bacteriostatic and bactericidal activity against MRSA, with a minimum inhibitory concentration of 4 µg/mL. It remains stable under a range of pH, temperatures, and serum, although it is susceptible to degradation by pepsin. Mechanistic investigations show that HfAMP compromises bacterial membranes by interacting with membrane components and disrupting the proton motive force, leading to metabolic disturbances. In a mouse model of MRSA-induced skin infection, HfAMP significantly reduced bacterial burden and inflammation in the affected skin tissues.
conclusionCollectively, these findings indicate that HfAMP possesses potent antibacterial activity against MRSA by compromising bacterial viability and inhibiting virulence, highlighting its potential as a promising candidate for the treatment of MRSA skin-infection.
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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.