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Antimicrobial activity of the indolicidin‐derived novel synthetic peptide In‐58

Natural peptides with antimicrobial activity are extremely diverse, and peptide synthesis technologies make it possible to significantly improve their properties for specific tasks. Here, we investigate the biological properties of the natural peptide indolicidin and the indolicidin‐derived novel sy... Full description

Journal Title: Journal of Peptide Science December 2017, Vol.23(12), pp.855-863
Main Author: Vasilchenko, A. S.
Other Authors: Vasilchenko, A. V. , Pashkova, T. M. , Smirnova, M. P. , Kolodkin, N. I. , Manukhov, I. V. , Zavilgelsky, G. B. , Sizova, E. A. , Kartashova, O. L. , Simbirtsev, A. S. , Rogozhin, E. A. , Duskaev, G. K. , Sycheva, M. V.
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ID: ISSN: 1075-2617 ; E-ISSN: 1099-1387 ; DOI: 10.1002/psc.3049
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recordid: wj10.1002/psc.3049
title: Antimicrobial activity of the indolicidin‐derived novel synthetic peptide In‐58
format: Article
creator:
  • Vasilchenko, A. S.
  • Vasilchenko, A. V.
  • Pashkova, T. M.
  • Smirnova, M. P.
  • Kolodkin, N. I.
  • Manukhov, I. V.
  • Zavilgelsky, G. B.
  • Sizova, E. A.
  • Kartashova, O. L.
  • Simbirtsev, A. S.
  • Rogozhin, E. A.
  • Duskaev, G. K.
  • Sycheva, M. V.
subjects:
  • Antimicrobial Peptides
  • Indolicidin
  • Synthetic Peptides
  • Mode Of Action
  • Biosensors
  • Bioluminescence
  • Sos Response
ispartof: Journal of Peptide Science, December 2017, Vol.23(12), pp.855-863
description: Natural peptides with antimicrobial activity are extremely diverse, and peptide synthesis technologies make it possible to significantly improve their properties for specific tasks. Here, we investigate the biological properties of the natural peptide indolicidin and the indolicidin‐derived novel synthetic peptide In‐58. In‐58 was generated by replacing all tryptophan residues on phenylalanine in D‐configuration; the α‐amino group in the main chain also was modified by unsaturated fatty acid. Compared with indolicidin, In‐58 is more bactericidal, more resistant to proteinase K, and less toxic to mammalian cells. Using molecular physics approaches, we characterized the action of In‐58 on bacterial cells at the cellular level. Also, we have found that studied peptides damage bacterial membranes. Using the luminescent biosensor strain MG1655 (), we investigated the action of indolicidin and In‐58 at the subcellular level. At subinhibitory concentrations, indolicidin and In‐58 induced an SOS response. Our data suggest that indolicidin damages the DNA, but bacterial membrane perturbation is its principal mode of action. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Peptide design. In‐58 was generated by replacing all L‐tryptophan residues on D‐phenylalanine; the α‐amino group in the main chain was modified by unsaturated fatty acid. Features of In‐58. 1) less toxic to mammalian cells, 2) more bactericidal, 3) more resistant to proteinase K. Mode of action. At subinhibitory concentrations indolicidin and In‐58 induced an SOS‐response. But bacterial membrane perturbation is its principal mode of action.
language:
source:
identifier: ISSN: 1075-2617 ; E-ISSN: 1099-1387 ; DOI: 10.1002/psc.3049
fulltext: fulltext
issn:
  • 1075-2617
  • 10752617
  • 1099-1387
  • 10991387
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titleAntimicrobial activity of the indolicidin‐derived novel synthetic peptide In‐58
creatorVasilchenko, A. S. ; Vasilchenko, A. V. ; Pashkova, T. M. ; Smirnova, M. P. ; Kolodkin, N. I. ; Manukhov, I. V. ; Zavilgelsky, G. B. ; Sizova, E. A. ; Kartashova, O. L. ; Simbirtsev, A. S. ; Rogozhin, E. A. ; Duskaev, G. K. ; Sycheva, M. V.
ispartofJournal of Peptide Science, December 2017, Vol.23(12), pp.855-863
identifier
subjectAntimicrobial Peptides ; Indolicidin ; Synthetic Peptides ; Mode Of Action ; Biosensors ; Bioluminescence ; Sos Response
descriptionNatural peptides with antimicrobial activity are extremely diverse, and peptide synthesis technologies make it possible to significantly improve their properties for specific tasks. Here, we investigate the biological properties of the natural peptide indolicidin and the indolicidin‐derived novel synthetic peptide In‐58. In‐58 was generated by replacing all tryptophan residues on phenylalanine in D‐configuration; the α‐amino group in the main chain also was modified by unsaturated fatty acid. Compared with indolicidin, In‐58 is more bactericidal, more resistant to proteinase K, and less toxic to mammalian cells. Using molecular physics approaches, we characterized the action of In‐58 on bacterial cells at the cellular level. Also, we have found that studied peptides damage bacterial membranes. Using the luminescent biosensor strain MG1655 (), we investigated the action of indolicidin and In‐58 at the subcellular level. At subinhibitory concentrations, indolicidin and In‐58 induced an SOS response. Our data suggest that indolicidin damages the DNA, but bacterial membrane perturbation is its principal mode of action. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Peptide design. In‐58 was generated by replacing all L‐tryptophan residues on D‐phenylalanine; the α‐amino group in the main chain was modified by unsaturated fatty acid. Features of In‐58. 1) less toxic to mammalian cells, 2) more bactericidal, 3) more resistant to proteinase K. Mode of action. At subinhibitory concentrations indolicidin and In‐58 induced an SOS‐response. But bacterial membrane perturbation is its principal mode of action.
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titleAntimicrobial activity of the indolicidin‐derived novel synthetic peptide In‐58
descriptionNatural peptides with antimicrobial activity are extremely diverse, and peptide synthesis technologies make it possible to significantly improve their properties for specific tasks. Here, we investigate the biological properties of the natural peptide indolicidin and the indolicidin‐derived novel synthetic peptide In‐58. In‐58 was generated by replacing all tryptophan residues on phenylalanine in D‐configuration; the α‐amino group in the main chain also was modified by unsaturated fatty acid. Compared with indolicidin, In‐58 is more bactericidal, more resistant to proteinase K, and less toxic to mammalian cells. Using molecular physics approaches, we characterized the action of In‐58 on bacterial cells at the cellular level. Also, we have found that studied peptides damage bacterial membranes. Using the luminescent biosensor strain MG1655 (), we investigated the action of indolicidin and In‐58 at the subcellular level. At subinhibitory concentrations, indolicidin and In‐58 induced an SOS response. Our data suggest that indolicidin damages the DNA, but bacterial membrane perturbation is its principal mode of action. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Peptide design. In‐58 was generated by replacing all L‐tryptophan residues on D‐phenylalanine; the α‐amino group in the main chain was modified by unsaturated fatty acid. Features of In‐58. 1) less toxic to mammalian cells, 2) more bactericidal, 3) more resistant to proteinase K. Mode of action. At subinhibitory concentrations indolicidin and In‐58 induced an SOS‐response. But bacterial membrane perturbation is its principal mode of action.
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titleAntimicrobial activity of the indolicidin‐derived novel synthetic peptide In‐58
authorVasilchenko, A. S. ; Vasilchenko, A. V. ; Pashkova, T. M. ; Smirnova, M. P. ; Kolodkin, N. I. ; Manukhov, I. V. ; Zavilgelsky, G. B. ; Sizova, E. A. ; Kartashova, O. L. ; Simbirtsev, A. S. ; Rogozhin, E. A. ; Duskaev, G. K. ; Sycheva, M. V.
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abstractNatural peptides with antimicrobial activity are extremely diverse, and peptide synthesis technologies make it possible to significantly improve their properties for specific tasks. Here, we investigate the biological properties of the natural peptide indolicidin and the indolicidin‐derived novel synthetic peptide In‐58. In‐58 was generated by replacing all tryptophan residues on phenylalanine in D‐configuration; the α‐amino group in the main chain also was modified by unsaturated fatty acid. Compared with indolicidin, In‐58 is more bactericidal, more resistant to proteinase K, and less toxic to mammalian cells. Using molecular physics approaches, we characterized the action of In‐58 on bacterial cells at the cellular level. Also, we have found that studied peptides damage bacterial membranes. Using the luminescent biosensor strain MG1655 (), we investigated the action of indolicidin and In‐58 at the subcellular level. At subinhibitory concentrations, indolicidin and In‐58 induced an SOS response. Our data suggest that indolicidin damages the DNA, but bacterial membrane perturbation is its principal mode of action. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Peptide design. In‐58 was generated by replacing all L‐tryptophan residues on D‐phenylalanine; the α‐amino group in the main chain was modified by unsaturated fatty acid. Features of In‐58. 1) less toxic to mammalian cells, 2) more bactericidal, 3) more resistant to proteinase K. Mode of action. At subinhibitory concentrations indolicidin and In‐58 induced an SOS‐response. But bacterial membrane perturbation is its principal mode of action.
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pages855-863
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date2017-12