Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity
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- Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity
- Other Titles
- 남극 어류 유래 4종 항균펩타이드의 특성 및 항균활성 분석연구
- Shweta Bharat Borkar
Sondavid K. Nandanwar
Lee, Jun Hyuck
Hak Jun Kim
- Antarctic eelpout; Antarctic notothenioid; cold-active peptide; disulfide bond; liver-expressed antimicrobial peptide
- Issue Date
- Shweta Bharat Borkar, et al. 2019. "Characterization of Four Liver-Expressed Antimicrobial Peptides from Antarctic Fish and Their Antibacterial Activity". APPLIED SCIENCES-BASEL, 9(20): 4299-4313.
- Abstract: Liver-expressed antimicrobial peptides (LEAPs) are cysteine-containing cationic peptides. LEAP-1 and LEAP-2 are eight- and four-cysteine containing antimicrobial peptides found in humans, respectively. LEAP-1 is a widely known antibacterial peptide involved in the innate immunity of fish, but the roles of LEAP-1 and LEAP-2 in Antarctic fish species such as notothenioid and eelpout are still unknown. In the present study, we synthesized and characterized novel LEAPs with four and eight cysteine residues, derived from Antarctic notothenioid (Dissostichus mawsoni) and Antarctic eelpout (Lycodichthys dearborni). Circular dichroism spectroscopy of these peptides showed a typical β-sheet confirmation. The LEAPs were found to be bactericidal against gram-positive as well as gram-negative bacteria. In the SYTOX green uptake assay, LEAPs did not trigger any significant increase in fluorescence. LEAPs competitively bind to DNA and replace the ethidium bromide (EB) dye. To determine the effect of temperature on LEAPs, we evaluated the antibacterial activity against Listeria monocytogenes at 5, 15, 25, and 35 °C. The results showed that the antibacterial activity of LEAPs decreases with an increase in temperature. Taken together, our results suggest that novel LEAPs with four and eight cysteine residues are bactericidal, with the likely mode of action being DNA binding.
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