Related Experiment Video
Updated: Aug 28, 2025

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
The antimicrobial effect of a novel peptide LL-1 on Escherichia coli by increasing membrane permeability
Lingling Zhou1,2, Kaiqi Lian2,3, Mengting Wang2
1College of Veterinary Medicine, Shanxi Agricultural University, Taigu, 030801, Shanxi, People's Republic of China.
Background:
The widespread use of antibiotics has led to the emergence of many drug-resistant strains; thus, the development of new antibacterial drugs is essential with antimicrobial peptides becoming the focus of research. This study assessed the antibacterial effect of a novel antimicrobial peptide, named LL-1 on Escherichia coli (E.coli) by determining the minimum inhibitory concentration (MIC) and the antibacterial curve. The interaction between LL-1 and E. coli DNA was then detected by nucleic acid gel electrophoresis. The effect of LL-1 on the E. coli cell membrane was assessed by detecting the leakage of β-galactosidase, nucleic acid and protein. The influence of LL-1 on the intracellular ATP of E. coli was analysed by determining the concentration of intracellular ATP. Finally, the bacteria and colonies of E. coli treated with LL-1 were observed using scanning and transmission electron microscopy.
Results:
The results suggested that the MIC value was 3.125 µg/ml, and the antibacterial effect was dose-dependent. LL-1 dose-dependently combined with E. coli DNA. LL-1 resulted in the leakage of intracellular β-galactosidase, nucleic acid and protein, and decreased intracellular ATP concentrations of E. coli. Two MIC of LL-1 caused E. coli to shrink, resulting in a rough surface, plasmolysis, and bacterial adhesion.
Conclusion:
This study indicated that LL-1 had a good bactericidal effect on E. coli by mainly increasing the permeability of the cell membrane, leading to leakage of the intracellular content. This will lay the foundation for an in-depth study on the antibacterial mechanism of LL-1 against E. coli and its clinical application.
Insights
A novel antimicrobial peptide, LL-1, effectively kills E. coli by damaging its cell membrane, causing leakage of essential components. This research highlights LL-1
Area of Science:
- Microbiology
- Biochemistry
- Drug Discovery
Background:
- Antibiotic resistance necessitates novel antibacterial agents.
- Antimicrobial peptides are a promising research area.
- Escherichia coli (E. coli) is a common target for antibacterial studies.
Purpose of the Study:
- To evaluate the antibacterial efficacy of a novel antimicrobial peptide, LL-1, against E. coli.
- To elucidate the mechanism of action of LL-1 on E. coli.
Main Methods:
- Minimum Inhibitory Concentration (MIC) determination.
- Nucleic acid gel electrophoresis to assess DNA interaction.
- Measurement of intracellular component leakage (β-galactosidase, nucleic acid, protein).
- Intracellular ATP concentration analysis.
- Scanning and transmission electron microscopy.
Main Results:
- LL-1 exhibited a Minimum Inhibitory Concentration (MIC) of 3.125 µg/ml against E. coli.
- LL-1 demonstrated dose-dependent antibacterial activity and DNA binding.
- LL-1 induced cell membrane permeability, leading to leakage of intracellular contents and reduced ATP levels.
- Electron microscopy revealed cell shrinkage, surface roughening, and plasmolysis in E. coli treated with LL-1.
Conclusions:
- LL-1 possesses significant bactericidal activity against E. coli.
- The primary mechanism involves disruption of the E. coli cell membrane.
- LL-1 shows potential for further investigation and clinical application as an antibacterial agent.
Related Concept Videos
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
Antimicrobial Effectiveness
Gene Regulation in Microbial Communities: Quorum Sensing

