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Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Antimicrobial Activity of Antimicrobial Peptide LPcin-YK3 Derived from Bovine Lactophoricin
Ji-Sun Kim1, Ji-Ho Jeong1, Jang-Hee Cho2
1Department of Chemistry, Hankuk University of Foreign Studies, Yong-In 17035, Republic of Korea.
Abstract:
We previously reported on lactophoricin (LPcin), a cationic α-helical antimicrobial peptide derived from bovine milk, which has antimicrobial effects on Candida albicans as well as Gram-positive and Gram-negative bacteria. In this study, we designed the LPcin-YK3 peptide, a shorter analog of LPcin, and investigated its antimicrobial activity. This peptide, consisting of 15 amino acids with + 3 net charges, was an effective antimicrobial agent against the on the Gram-positive strain, Staphylococcus aureus (MIC: 0.62 μg/ml). In addition, the hemolytic activity assay revealed that the peptide was not toxic to mouse and human erythrocytes up to 40 μg/ml. We also used circular dichroism spectroscopy to confirm that peptide in the presence of lipid has α-helical structures and later provide an overview of the relationship between each structure and antimicrobial activity. This peptide is a member of a new class of antimicrobial agents that could potentially overcome the problem of bacterial resistance caused by overuse of conventional antibiotics. Therefore, it could be used as a therapeutic or natural additive, particularly in the cosmetics industry.
Insights
A new bovine milk-derived peptide, LPcin-YK3, shows strong antimicrobial activity against Staphylococcus aureus. This safe and effective peptide may offer a solution to antibiotic resistance, particularly for the cosmetics industry.
Area of Science:
- Biochemistry
- Microbiology
- Peptide Science
Background:
- Lactophoricin (LPcin) is a bovine milk-derived antimicrobial peptide with broad-spectrum activity.
- Antimicrobial resistance necessitates the development of novel therapeutic agents.
Purpose of the Study:
- To design and evaluate a shorter analog of LPcin, named LPcin-YK3.
- To assess the antimicrobial efficacy and safety profile of LPcin-YK3.
Main Methods:
- LPcin-YK3, a 15-amino acid peptide, was synthesized and its antimicrobial activity determined via Minimum Inhibitory Concentration (MIC) assays.
- Hemolytic activity assays were performed using mouse and human erythrocytes.
- Circular dichroism spectroscopy was employed to analyze peptide structure in the presence of lipids.
Main Results:
- LPcin-YK3 demonstrated potent antimicrobial activity against Staphylococcus aureus with an MIC of 0.62 μg/ml.
- The peptide exhibited no toxicity to erythrocytes at concentrations up to 40 μg/ml.
- Circular dichroism confirmed the formation of α-helical structures in the presence of lipids, correlating with antimicrobial action.
Conclusions:
- LPcin-YK3 is a potent and safe antimicrobial peptide with potential therapeutic applications.
- This peptide represents a promising new class of agents to combat antibiotic resistance.
- LPcin-YK3 could be utilized as a therapeutic or natural additive, especially in the cosmetics sector.
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