ArticleThe Journal of biological chemistry2010
Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 230 citations in OpenAlex.
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- Short Antimicrobial Peptides Based on Arginine and Tryptophan: Agents with Potential in Combating Resistant Pathogens.ACS omega · 2026Article
- Characterizing interactions of Staphylococcus aureus and Escherichia coli in dual-species implant-associated biofilms.NPJ biofilms and microbiomes · 2025Article
- Modifying Antifungal Peptides as Safe Food Preservatives.Journal of agricultural and food chemistry · 2025Article
- Antimicrobial Action of Essential Oil ofAntibiotics (Basel, Switzerland) · 2025Article
- Nanoplastics-mediated physiologic and genomic responses in pathogenic Escherichia coli O157:H7.Journal of nanobiotechnology · 2025Article
- Selectivity of membrane-active peptides: the role of electrostatics and other membrane biophysical properties.Biophysical reviews · 2025Review
- Cell wall polysaccharide alters the surface electric potential ofCurrent research in microbial sciences · 2025Article
- Single Disulfide Bond in Host Defense Thanatin Analog Peptides: Antimicrobial Activity, Atomic-Resolution Structures and Target Interactions.International journal of molecular sciences · 2024Article
- Dual Antimicrobial and Anticancer Activity of Membrane-Active Peptide BP52.The protein journal · 2024Article
- 1,3,5-Triazine as Branching Connector for the Construction of Novel Antimicrobial Peptide Dendrimers: Synthesis and Biological Characterization.International journal of molecular sciences · 2024Article
- Triggered Release of Ampicillin from Metallic Implant Coatings for Combating Periprosthetic Infections.ACS applied materials & interfaces · 2024Article
- Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100.International journal of molecular sciences · 2024Review
- Outer-Membrane Permeabilization, LPS Transport Inhibition: Activity, Interactions, and Structures of Thanatin Derived Antimicrobial Peptides.International journal of molecular sciences · 2024Article
- Structures, Interactions and Activity of the N-Terminal Truncated Variants of Antimicrobial Peptide Thanatin.Antibiotics (Basel, Switzerland) · 2024Article
- In Silico and In vitro Evaluations of the Antibacterial Activities of HIV-1 Nef Peptides againstInternational journal of molecular and cellular medicine · 2024Article
- Leptospiral adhesins: from identification to future perspectives.Frontiers in microbiology · 2024Review
- Quantitative Imaging of the Action of vCPP2319, an Antimicrobial Peptide from a Viral Scaffold, againstACS infectious diseases · 2023Article
- LL37-Derived Fragments Improve the Antibacterial Potential of Penicillin G and Ampicillin against Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2023Article
26 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The potential of antimicrobial peptides (AMPs) as an alternative to conventional therapies is well recognized. Insights into the biological and biophysical properties of AMPs are thus key to understanding their mode of action. In this study, the mechanisms adopted by two AMPs in disrupting the gram-negative Escherichia coli bacterial envelope were explored. BP100 is a short cecropin A-melittin hybrid peptide known to inhibit the growth of phytopathogenic gram-negative bacteria. pepR, on the other hand, is a novel AMP derived from the dengue virus capsid protein. Both BP100 and pepR were found to inhibit the growth of E. coli at micromolar concentrations. Zeta potential measurements of E. coli incubated with increasing peptide concentrations allowed for the establishment of a correlation between the minimal inhibitory concentration (MIC) of each AMP and membrane surface charge neutralization. While a neutralization-mediated killing mechanism adopted by either AMP is not necessarily implied, the hypothesis that surface neutralization occurs close to MIC values was confirmed. Atomic force microscopy (AFM) was then employed to visualize the structural effect of the interaction of each AMP with the E. coli cell envelope. At their MICs, BP100 and pepR progressively destroyed the bacterial envelope, with extensive damage already occurring 2 h after peptide addition to the bacteria. A similar effect was observed for each AMP in the concentration-dependent studies. At peptide concentrations below MIC values, only minor disruptions of the bacterial surface occurred.
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