Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus

Previous studies had identified novel antimicrobial peptides derived from witch flounder. In this work, we extended the search for the activity of peptide that showed antibacterial activity on clinically isolated bacterial cells and bacterial biofilm. Pseudomonas aeruginosa was obtained from otitis...

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Main Authors: Chang Ho Seo, Yoonkyung Park, Myeong-Sun Kim, Young Gwon Kim, Ramamourthy Gopal, Jun Ho Lee
Format: Article
Language:English
Published: MDPI AG 2013-05-01
Series:Marine Drugs
Subjects:
Online Access:http://www.mdpi.com/1660-3397/11/6/1836
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author Chang Ho Seo
Yoonkyung Park
Myeong-Sun Kim
Young Gwon Kim
Ramamourthy Gopal
Jun Ho Lee
author_facet Chang Ho Seo
Yoonkyung Park
Myeong-Sun Kim
Young Gwon Kim
Ramamourthy Gopal
Jun Ho Lee
author_sort Chang Ho Seo
collection DOAJ
description Previous studies had identified novel antimicrobial peptides derived from witch flounder. In this work, we extended the search for the activity of peptide that showed antibacterial activity on clinically isolated bacterial cells and bacterial biofilm. Pseudomonas aeruginosa was obtained from otitis media and cholelithiasis patients, while Staphylococcus aureus was isolated from otitis media patients. We found that synthetic peptide NRC-16 displays antimicrobial activity and is not sensitive to salt during its bactericidal activity. Interestingly, this peptide also led to significant inhibition of biofilm formation at a concentration of 4–16 μM. NRC-16 peptide is able to block biofilm formation at concentrations just above its minimum inhibitory concentration while conventional antibiotics did not inhibit the biofilm formation except ciprofloxacin and piperacillin. It did not cause significant lysis of human RBC, and is not cytotoxic to HaCaT cells and RAW264.7 cells, thereby indicating its selective antimicrobial activity. In addition, the peptide’s binding and permeation activities were assessed by tryptophan fluorescence, calcein leakage and circular dichroism using model mammalian membranes composed of phosphatidylcholine (PC), PC/cholesterol (CH) and PC/sphingomyelin (SM). These experiments confirmed that NRC-16 does not interact with any of the liposomes but the control peptide melittin did. Taken together, we found that NRC-16 has potent antimicrobial and antibiofilm activities with less cytotoxicity, and thus can be considered for treatment of microbial infection in the future.
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spelling doaj.art-ad51a5b450194480bc74edf0e7b37bac2022-12-22T01:59:18ZengMDPI AGMarine Drugs1660-33972013-05-011161836185210.3390/md11061836Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossusChang Ho SeoYoonkyung ParkMyeong-Sun KimYoung Gwon KimRamamourthy GopalJun Ho LeePrevious studies had identified novel antimicrobial peptides derived from witch flounder. In this work, we extended the search for the activity of peptide that showed antibacterial activity on clinically isolated bacterial cells and bacterial biofilm. Pseudomonas aeruginosa was obtained from otitis media and cholelithiasis patients, while Staphylococcus aureus was isolated from otitis media patients. We found that synthetic peptide NRC-16 displays antimicrobial activity and is not sensitive to salt during its bactericidal activity. Interestingly, this peptide also led to significant inhibition of biofilm formation at a concentration of 4–16 μM. NRC-16 peptide is able to block biofilm formation at concentrations just above its minimum inhibitory concentration while conventional antibiotics did not inhibit the biofilm formation except ciprofloxacin and piperacillin. It did not cause significant lysis of human RBC, and is not cytotoxic to HaCaT cells and RAW264.7 cells, thereby indicating its selective antimicrobial activity. In addition, the peptide’s binding and permeation activities were assessed by tryptophan fluorescence, calcein leakage and circular dichroism using model mammalian membranes composed of phosphatidylcholine (PC), PC/cholesterol (CH) and PC/sphingomyelin (SM). These experiments confirmed that NRC-16 does not interact with any of the liposomes but the control peptide melittin did. Taken together, we found that NRC-16 has potent antimicrobial and antibiofilm activities with less cytotoxicity, and thus can be considered for treatment of microbial infection in the future.http://www.mdpi.com/1660-3397/11/6/1836fish peptideNRC-16antimicrobial peptideantibiofilm peptideeukaryotic membranephosphatidylcholinecholesterolsphingomyelin
spellingShingle Chang Ho Seo
Yoonkyung Park
Myeong-Sun Kim
Young Gwon Kim
Ramamourthy Gopal
Jun Ho Lee
Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
Marine Drugs
fish peptide
NRC-16
antimicrobial peptide
antibiofilm peptide
eukaryotic membrane
phosphatidylcholine
cholesterol
sphingomyelin
title Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
title_full Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
title_fullStr Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
title_full_unstemmed Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
title_short Anti-Microbial, Anti-Biofilm Activities and Cell Selectivity of the NRC-16 Peptide Derived from Witch Flounder, Glyptocephalus cynoglossus
title_sort anti microbial anti biofilm activities and cell selectivity of the nrc 16 peptide derived from witch flounder glyptocephalus cynoglossus
topic fish peptide
NRC-16
antimicrobial peptide
antibiofilm peptide
eukaryotic membrane
phosphatidylcholine
cholesterol
sphingomyelin
url http://www.mdpi.com/1660-3397/11/6/1836
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