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Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
HJH-1, a Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity Antimicrobial Peptide
Qing Wang1,2, Yanzhao Xu3, Mengmeng Dong4
1College of Animal Science and Technology, Shihezi University, Shihezi 832003, China. wangqing@hist.edu.cn.
Abstract:
With the overuse of antibiotics, multidrug-resistant bacteria pose a significant threat to human health. Antimicrobial peptides (AMPs) are a promising alternative to conventional antibiotics. This study examines the antimicrobial and membrane activity of HJH-1, a cationic peptide derived from the hemoglobin α-subunit of bovine erythrocytes P3. HJH-1 shows potent antimicrobial activity against different bacterial species associated with infection and causes weaker hemolysis of erythrocytes, at least five times the minimum inhibitory concentration (MIC). HJH-1 has good stability to tolerance temperature, pH value, and ionic strength. The anionic membrane potential probe bis-(1,3-dibutylbarbituric acid) trimethine oxonol [DiBAC₄(3)] and propidium iodide are used as indicators of membrane integrity. In the presence of HJH-1 (1× MIC), Escherichiacoli membranes rapidly depolarise, whereas red blood cells show gradual hyperpolarisation. Scanning electron microscopy and transmission electron micrographs show that HJH-1 (1× MIC) damaged the membranes of Escherichia coli, Staphylococcus aureus, and Candida albicans. In conclusion, HJH-1 damages the integrity of the bacterial membrane, preventing the growth of bacteria. HJH-1 has broad-spectrum antibacterial activity, and these activities are performed by changing the normal cell transmembrane potential and disrupting the integrity of the bacterial membrane.
Insights
This study shows that HJH-1, an antimicrobial peptide, effectively damages bacterial membranes, offering a potential alternative to antibiotics against multidrug-resistant bacteria.
Area of Science:
- Biochemistry
- Microbiology
- Biophysics
Background:
- Overuse of antibiotics has led to multidrug-resistant bacteria, a major global health threat.
- Antimicrobial peptides (AMPs) are emerging as a promising alternative to conventional antibiotics due to their novel mechanisms of action.
- Bovine hemoglobin-derived peptides represent a potential source of new AMPs.
Purpose of the Study:
- To investigate the antimicrobial activity and membrane-disrupting effects of HJH-1, a cationic peptide derived from bovine hemoglobin.
- To assess the safety profile of HJH-1 concerning erythrocyte hemolysis.
- To evaluate the stability of HJH-1 under various environmental conditions.
Main Methods:
- Minimum Inhibitory Concentration (MIC) assays against various bacterial and fungal species.
- Hemolysis assays using erythrocytes.
- Membrane potential assays using DiBAC₄(3) and propidium iodide.
- Microscopy techniques (SEM, TEM) to visualize membrane damage.
Main Results:
- HJH-1 demonstrated potent broad-spectrum antimicrobial activity against tested bacteria and Candida albicans.
- HJH-1 exhibited significantly lower hemolytic activity compared to its antimicrobial concentrations.
- HJH-1 induced rapid depolarization of bacterial membranes (E. coli) and hyperpolarization of red blood cells.
- Microscopy confirmed membrane damage in E. coli, S. aureus, and C. albicans upon HJH-1 treatment.
- HJH-1 showed good stability across a range of temperatures, pH values, and ionic strengths.
Conclusions:
- HJH-1 effectively disrupts bacterial membrane integrity, leading to cell death and inhibiting microbial growth.
- HJH-1 possesses broad-spectrum antimicrobial properties with a favorable safety profile regarding erythrocyte lysis.
- The mechanism of action involves altering transmembrane potential and damaging the bacterial membrane, making HJH-1 a promising candidate for combating multidrug-resistant pathogens.
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