ArticlePloS one2014
Importance of Tryptophan in Transforming an Amphipathic Peptide into a Pseudomonas aeruginosa-Targeted Antimicrobial Peptide.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 45 citations in OpenAlex.
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- Antimicrobial Peptides: Potential Therapeutics Against Drug-Resistant Pulmonary Infections.Archivos de bronconeumologia · 2022Article
- KDEON WK-11: A short antipseudomonal peptide with promising potential.Frontiers in chemistry · 2022Article
- A Novel Peptide Derived from the Transmembrane Domain of Romo1 Is a Promising Candidate for Sepsis Treatment and Multidrug-Resistant Bacteria.International journal of molecular sciences · 2021Article
- Engineering Selectively Targeting Antimicrobial Peptides.Annual review of biomedical engineering · 2021Review
- The Trp-rich Antimicrobial Amphiphiles With Intramolecular Aromatic Interactions for the Treatment of Bacterial Infection.Frontiers in microbiology · 2021Article
- Peptides With Triplet-Tryptophan-Pivot Promoted Pathogenic Bacteria Membrane Defects.Frontiers in microbiology · 2020Article
- Sarconesin II, a New Antimicrobial Peptide Isolated fromMolecules (Basel, Switzerland) · 2019Article
- A Pilot Study of the Synergy between Two Antimicrobial Peptides and Two Common Antibiotics.Antibiotics (Basel, Switzerland) · 2019Article
- Comparative mode of action of the antimicrobial peptide melimine and its derivative Mel4 against Pseudomonas aeruginosa.Scientific reports · 2019Article
- Mode of action of the antimicrobial peptide Mel4 is independent of Staphylococcus aureus cell membrane permeability.PloS one · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we found that simple substitution of amino acids in the middle position of the hydrophobic face of an amphipathic peptide RI16 with tryptophan (T9W) considerably transformed into an antimicrobial peptide specifically targeting Pseudomonas aeruginosa. Minimal inhibitory concentration (MIC) results demonstrated that T9W had a strong and specifically antimicrobial activity against P. aeruginosa, including antibiotic-resistant strains, but was not active against Escherichia coli, Salmonella typhimurium, Staphylococcus aureus and Staphyfococcus epidermidis. Fluorescent spectroscopic assays indicated that T9W interacted with the membrane of P. aeruginosa, depolarizing the outer and the inner membrane of bacterial cells. Salt susceptibility assay showed that T9W still maintained its strong anti-pseudomonas activity in the presence of salts at physiological concentrations, and in hemolytic and MTT assays T9W also showed no toxicity against human blood cells and macrophages. In vivo assay demonstrated that T9W also displayed no toxicity to Chinese Kun Ming (KM) mice. Furthermore, the strong antibiofilm activity was also observed with the peptide T9W, which decreased the percentage of biomass formation in a dose-dependent manner. Overall, these findings indicated that design of single-pathogen antimicrobial agents can be achieved by simple amino acid mutation in naturally occurring peptide sequences and this study suggested a model of optimization/design of anti-pseudomonas drugs in which the tryptophan residue was a conserved element.
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