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On the Antimicrobial Activity of Various Peptide-Based Dendrimers of Similar Architecture

Lind, Tania LU ; Polcyn, Piotr; Zielinska, Paulina; Cardenas, Marite and Urbanczyk-Lipkowska, Zofia (2015) In Molecules 20(1). p.738-753
Abstract
Antimicrobial drug resistance is a major human health threat. Among the many attempts to tackle this problem, the synthesis of antimicrobial compounds that mimic natural antimicrobial peptides appears as a promising approach. Peptide-based dendrimers can be designed to have higher potency than natural antimicrobial peptides and at the same time they can evade the bacterial defense system. Novel dendrimers with similar chemical structure but varying potency in terms of minimum inhibitory concentration were designed. The dependency between dendrimer structure and antibacterial activity as well as their capacity to attack model cell membranes was studied. The data suggests that supramolecular structure in terms of charge distribution and... (More)
Antimicrobial drug resistance is a major human health threat. Among the many attempts to tackle this problem, the synthesis of antimicrobial compounds that mimic natural antimicrobial peptides appears as a promising approach. Peptide-based dendrimers can be designed to have higher potency than natural antimicrobial peptides and at the same time they can evade the bacterial defense system. Novel dendrimers with similar chemical structure but varying potency in terms of minimum inhibitory concentration were designed. The dependency between dendrimer structure and antibacterial activity as well as their capacity to attack model cell membranes was studied. The data suggests that supramolecular structure in terms of charge distribution and amphiphilicity, rather than net charge, is the main driver for disruption of cellular membranes and this correlates well with dendrimer hemolytic activity. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
dendrimers, peptide, antimicrobial, lipids
in
Molecules
volume
20
issue
1
pages
738 - 753
publisher
Molecular Diversity Preservation International
external identifiers
  • wos:000348319000043
  • scopus:84921523986
ISSN
1420-3049
DOI
10.3390/molecules20010738
language
English
LU publication?
yes
id
8167d2ef-0a10-449b-b508-7e4eff621a66 (old id 5204218)
date added to LUP
2015-03-25 15:49:59
date last changed
2017-11-12 03:35:13
@article{8167d2ef-0a10-449b-b508-7e4eff621a66,
  abstract     = {Antimicrobial drug resistance is a major human health threat. Among the many attempts to tackle this problem, the synthesis of antimicrobial compounds that mimic natural antimicrobial peptides appears as a promising approach. Peptide-based dendrimers can be designed to have higher potency than natural antimicrobial peptides and at the same time they can evade the bacterial defense system. Novel dendrimers with similar chemical structure but varying potency in terms of minimum inhibitory concentration were designed. The dependency between dendrimer structure and antibacterial activity as well as their capacity to attack model cell membranes was studied. The data suggests that supramolecular structure in terms of charge distribution and amphiphilicity, rather than net charge, is the main driver for disruption of cellular membranes and this correlates well with dendrimer hemolytic activity.},
  author       = {Lind, Tania and Polcyn, Piotr and Zielinska, Paulina and Cardenas, Marite and Urbanczyk-Lipkowska, Zofia},
  issn         = {1420-3049},
  keyword      = {dendrimers,peptide,antimicrobial,lipids},
  language     = {eng},
  number       = {1},
  pages        = {738--753},
  publisher    = {Molecular Diversity Preservation International},
  series       = {Molecules},
  title        = {On the Antimicrobial Activity of Various Peptide-Based Dendrimers of Similar Architecture},
  url          = {http://dx.doi.org/10.3390/molecules20010738},
  volume       = {20},
  year         = {2015},
}