ArticlePloS one2013
A peptide derived from phage display library exhibits antibacterial activity against E. coli and Pseudomonas aeruginosa.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- Antimicrobial cyclic peptides effectively inhibit multiple forms of Borrelia and cross the blood-brain barrier model.Scientific reports · 2025Article
- Targeted Killing of Staphylococcus aureus Using Specific Peptides Displayed on Yeast Vacuoles.Microbiology spectrum · 2023Article
- Strategies and opportunities for engineering antifungal peptides for therapeutic applications.Current opinion in biotechnology · 2023Review
- Phage Display-Derived Peptides and Antibodies for Bacterial Infectious Diseases Therapy and Diagnosis.Molecules (Basel, Switzerland) · 2023Review
- Development of a Novel Antibacterial Peptide, PAM-5, via Combination of Phage Display Selection and Computer-Assisted Modification.Biomolecules · 2023Article
- Recent Advances on Peptide-Based Biosensors and Electronic Noses for Foodborne Pathogen Detection.Biosensors · 2023Review
- Chemical-Biology and Metabolomics Studies in Phage-Host Interactions.Advances in experimental medicine and biology · 2023Article
- Synergy by Perturbing the Gram-Negative Outer Membrane: Opening the Door for Gram-Positive Specific Antibiotics.ACS infectious diseases · 2022Review
- Elucidating the mechanism by which synthetic helper peptides sensitize Pseudomonas aeruginosa to multiple antibiotics.PLoS pathogens · 2021Article
- Human Hexa-Histidine-Tagged Single-Chain Variable Fragments for Bioimaging of Bacterial Infections.ACS omega · 2021Article
- Lipidation of Antimicrobial Peptides as a Design Strategy for Future Alternatives to Antibiotics.International journal of molecular sciences · 2020Review
- Analysis of antibacterial and antibiofilm activity of purified recombinant Azurin fromIranian journal of microbiology · 2019Article
- Reassessing the Host Defense Peptide Landscape.Frontiers in chemistry · 2019Review
- Screening of bacteria-binding peptides and one-pot ZnO surface modification for bacterial cell entrapment.RSC advances · 2018Article
- Article
- Metacaspase-binding peptide inhibits heat shock-induced death in Leishmania (L.) amazonensis.Cell death & disease · 2017Article
- Novel cationic peptide TP359 down-regulates the expression of outer membrane biogenesis genes in Pseudomonas aeruginosa: a potential TP359 anti-microbial mechanism.BMC microbiology · 2016Article
- Potentiating the Activity of Nisin against Escherichia coli.Frontiers in cell and developmental biology · 2016Article
- Article
- Epinecidin-1 has immunomodulatory effects, facilitating its therapeutic use in a mouse model of Pseudomonas aeruginosa sepsis.Antimicrobial agents and chemotherapy · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Emergence of drug resistant strains to currently available antibiotics has resulted in the quest for novel antimicrobial agents. Antimicrobial peptides (AMPs) are receiving attention as alternatives to antibiotics. In this study, we used phage-display random peptide library to identify peptides binding to the cell surface of E. coli. The peptide with sequence RLLFRKIRRLKR (EC5) bound to the cell surface of E. coli and exhibited certain features common to AMPs and was rich in Arginine and Lysine residues. Antimicrobial activity of the peptide was tested in vitro by growth inhibition assays and the bacterial membrane permeabilization assay. The peptide was highly active against gram-negative organisms and showed significant bactericidal activity against E. coli and P. aeruginosa resulting in a reduction of 5 log(10) CFU/ml. In homologous plasma and platelets, incubation of EC5 with the bacteria resulted in significant reduction of E. coli and P. aeruginosa, compared to the peptide-free controls. The peptide was non-hemolytic and non-cytotoxic when tested on eukaryotic cells in culture. EC5 was able to permeabilize the outer membrane of E. coli and P. aeruginosa causing rapid depolarization of cytoplasmic membrane resulting in killing of the cells at 5 minutes of exposure. The secondary structure of the peptide showed a α-helical conformation in the presence of aqueous environment. The bacterial lipid interaction with the peptide was also investigated using Molecular Dynamic Simulations. Thus this study demonstrates that peptides identified to bind to bacterial cell surface through phage-display screening may additionally aid in identifying and developing novel antimicrobial peptides.
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