ArticleAMB Express2019
Mechanism of action of antimicrobial peptide P5 truncations against Pseudomonas aeruginosa and Staphylococcus aureus.
Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Genome-Guided Discovery of an Antimicrobial Peptide Scaffold from an Undescribed AntarcticInternational journal of molecular sciences · 2026Article
- Identification and Optimization of a Truncated Hs-1-Derived Antimicrobial Peptide for Enhanced Broad-Spectrum Antiviral Activity.ChemMedChem · 2026Article
- Antimicrobial Peptides as Antibiotic Adjuvants: Overcoming Resistance through Multifaceted Mechanisms.Probiotics and antimicrobial proteins · 2026Article
- From computational screening toFrontiers in microbiology · 2026Article
- Antibacterial and antibiofilm activity of nanoparticles inRSC advances · 2025Article
- Structure-function relationship of the Pseudomonas aeruginosa AsmA-like proteins YhdP and YdbH involved in outer membrane biogenesis.Protein science : a publication of the Protein Society · 2025Article
- Retargeting Gram-Positive-Only Adarotene-Derived Antibacterials to Broad-Spectrum Antibiotics.Antibiotics (Basel, Switzerland) · 2025Article
- Reconstructing the Antibiotic Pipeline: Natural Alternatives to Antibacterial Agents.Biomolecules · 2025Review
- Repurposed Anti-Multiple Sclerosis Drug Fty720 Targets Carbapenem-Resistant Acinetobacter baumannii via Multiple Pathways.Current microbiology · 2024Article
- Innovative Strategies and Methodologies in Antimicrobial Peptide Design.Journal of functional biomaterials · 2024Review
- Antibacterial efficacy and membrane mechanism of action of theMicrobiology spectrum · 2024Article
- Mechanistic Study of Antimicrobial Effectiveness of Cyclic Amphipathic Peptide [RAntibiotics (Basel, Switzerland) · 2024Article
- Redundant essentiality of AsmA-like proteins inmSphere · 2024Article
- LL37-Derived Fragments Improve the Antibacterial Potential of Penicillin G and Ampicillin against Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2023Article
- Synergistic Effect, Improved Cell Selectivity, and Elucidating the Action Mechanism of Antimicrobial Peptide YS12.International journal of molecular sciences · 2023Article
- Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (International journal of molecular sciences · 2023Article
- In vitro and in vivo antibiofilm activity of the synthetic antimicrobial peptide WLBU2 against multiple drug resistant Pseudomonas aeruginosa strains.BMC microbiology · 2023Article
- Rational design of stapled antimicrobial peptides.Amino acids · 2023Review
- A Novel Antimicrobial Peptide SpampcinInternational journal of molecular sciences · 2022Article
- Novel D-form of hybrid peptide (D-AP19) rapidly kills Acinetobacter baumannii while tolerating proteolytic enzymes.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rates of microbial drug resistance are increasing worldwide; therefore, antimicrobial peptides (AMPs) are considered promising alternative therapeutic agents to antibiotics. AMPs are essential components of the innate immune system and exhibit broad-spectrum antimicrobial activity. P5 is a Cecropin A-Magainin 2 hybrid analog peptide with antimicrobial activity against Gram-negative and Gram-positive bacteria. In the present study, truncated peptides were designed to reduction length, retainment their antimicrobial activity and low toxicity at high concentrations compared with that of the parent peptide P5. The truncated peptides P5-CT1 and P5-NT1 exhibited antibacterial activities against both Gram-negative and Gram-positive bacteria. In contrast, P5-CT2, P5-CT3, P5-NT2, and P5-NT3 showed higher antibacterial activities against gram-positive bacteria compared to Gram-negative bacteria at low concentration of peptides. The truncated peptides showed lower hemolytic activity and toxic effects against mammalian cells compared with those of the parent peptide P5. The levels of several truncated peptides were maintained in the presence of physiological concentrations of salts, indicating their high stability. The results of flow cytometry, propidium iodide uptake, n-phenyl-1-naphthylamine uptake, and 3,3'-dipropylthiadicarbocyanine iodide assays showed that these truncated peptides killed microbial cells by increasing membrane permeability, thereby causing membrane damage. The results suggested that truncated peptides of P5 have good potential for use as novel antimicrobial agents.
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