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Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities
MicrocinJ25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E. coli. The present study focuses on preparation and evaluation of in-vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Shaheed Beheshti University of Medical Sciences
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6934971/ https://www.ncbi.nlm.nih.gov/pubmed/32641937 http://dx.doi.org/10.22037/ijpr.2019.1100750 |
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author | Mazaheri Tehrani, Maryam Erfani, Mostafa Amirmozafari, Nour Nejadsattari, Taher |
author_facet | Mazaheri Tehrani, Maryam Erfani, Mostafa Amirmozafari, Nour Nejadsattari, Taher |
author_sort | Mazaheri Tehrani, Maryam |
collection | PubMed |
description | MicrocinJ25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E. coli. The present study focuses on preparation and evaluation of in-vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared a MccJ25-derived peptide containing 14 amino acids and a single intra-molecular disulfide bond according to solid phase synthesis strategy. The purified peptide was characterized by Liquid chromatography-mass spectrometry (LC-MS) and Fourier Transform Infrared (FTIR) spectroscopy. 96-well microdilution plate assay was exerted for determination of minimum inhibitory concentration (MIC) of peptide against different bacterial strains. Cytotoxicity of the peptide derivative on HT-29 cell line assayed using MTT test. The final peptide successfully was prepared with purity more than 99.8% as determined by analytical HPLC. The evaluation of antibacterial activity of the peptide against Gram-positive and Gram- negative bacteria revealed that the peptide was very effective against E. coli 35218 with minimum inhibitory concentration (MIC) at dose 3.9 µM. The hemolytic activity toward human erythrocytes was very minimal below 0.3%. The cell viability percentage of HT-29 cell line after 24 h of contact with the peptide was more than 83%. The high sensitivity of E. coli strain to this new peptide derived from MccJ25 and through minimal toxicity to cancerous cell, suggesting that above synthesized peptide could be considered as a bioactive compound for further investigations. |
format | Online Article Text |
id | pubmed-6934971 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Shaheed Beheshti University of Medical Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-69349712020-07-07 Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities Mazaheri Tehrani, Maryam Erfani, Mostafa Amirmozafari, Nour Nejadsattari, Taher Iran J Pharm Res Original Article MicrocinJ25 (MccJ25) is a small ribosomally synthesized antimicrobial peptide that is produced by Enterobacteriacea family especially E. coli. The present study focuses on preparation and evaluation of in-vitro antimicrobial and biological properties of a new peptide derived from MccJ25. We prepared a MccJ25-derived peptide containing 14 amino acids and a single intra-molecular disulfide bond according to solid phase synthesis strategy. The purified peptide was characterized by Liquid chromatography-mass spectrometry (LC-MS) and Fourier Transform Infrared (FTIR) spectroscopy. 96-well microdilution plate assay was exerted for determination of minimum inhibitory concentration (MIC) of peptide against different bacterial strains. Cytotoxicity of the peptide derivative on HT-29 cell line assayed using MTT test. The final peptide successfully was prepared with purity more than 99.8% as determined by analytical HPLC. The evaluation of antibacterial activity of the peptide against Gram-positive and Gram- negative bacteria revealed that the peptide was very effective against E. coli 35218 with minimum inhibitory concentration (MIC) at dose 3.9 µM. The hemolytic activity toward human erythrocytes was very minimal below 0.3%. The cell viability percentage of HT-29 cell line after 24 h of contact with the peptide was more than 83%. The high sensitivity of E. coli strain to this new peptide derived from MccJ25 and through minimal toxicity to cancerous cell, suggesting that above synthesized peptide could be considered as a bioactive compound for further investigations. Shaheed Beheshti University of Medical Sciences 2019 /pmc/articles/PMC6934971/ /pubmed/32641937 http://dx.doi.org/10.22037/ijpr.2019.1100750 Text en This is an Open Access article distributed under the terms of the Creative Commons Attribution License, (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Article Mazaheri Tehrani, Maryam Erfani, Mostafa Amirmozafari, Nour Nejadsattari, Taher Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title | Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title_full | Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title_fullStr | Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title_full_unstemmed | Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title_short | Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities |
title_sort | synthesis of a peptide derivative of microcinj25 and evaluation of antibacterial and biological activities |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6934971/ https://www.ncbi.nlm.nih.gov/pubmed/32641937 http://dx.doi.org/10.22037/ijpr.2019.1100750 |
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