Effect of hydrophobic modifications in antimicrobial peptides.
(2013) In Advances in Colloid and Interface Science- Abstract
- With increasing resistance development against conventional antibiotics, there is an urgent need to identify novel approaches for infection treatment. Antimicrobial peptides may offer opportunities in this context, hence there has been considerable interest in identification and optimization of such peptides during the last decade in particular, with the long-term aim of developing these to potent and safe therapeutics. In the present overview, focus is placed on hydrophobic modifications of antimicrobial peptides, and how these may provide opportunities to combat also more demanding pathogens, including multi-resistant strains, yet not provoking unacceptable toxic responses. In doing so, physicochemical factors affecting peptide... (More)
- With increasing resistance development against conventional antibiotics, there is an urgent need to identify novel approaches for infection treatment. Antimicrobial peptides may offer opportunities in this context, hence there has been considerable interest in identification and optimization of such peptides during the last decade in particular, with the long-term aim of developing these to potent and safe therapeutics. In the present overview, focus is placed on hydrophobic modifications of antimicrobial peptides, and how these may provide opportunities to combat also more demanding pathogens, including multi-resistant strains, yet not provoking unacceptable toxic responses. In doing so, physicochemical factors affecting peptide interactions with bacterial and eukaryotic cell membranes are discussed. Throughout, an attempt is made to illustrate how physicochemical studies on model lipid membranes can be correlated to result from bacterial and cell assays, and knowledge from this translated into therapeutic considerations. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4006234
- author
- Schmidtchen, Artur LU ; Pasupuleti, Mukesh LU and Malmsten, Martin LU
- organization
- publishing date
- 2013-07-05
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Advances in Colloid and Interface Science
- publisher
- Elsevier
- external identifiers
-
- pmid:23910480
- wos:000333780600020
- scopus:84903362494
- pmid:23910480
- ISSN
- 1873-3727
- DOI
- 10.1016/j.cis.2013.06.009
- language
- English
- LU publication?
- yes
- id
- 21f31a83-7c7d-4b79-892b-2e06fc34f0cf (old id 4006234)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/23910480?dopt=Abstract
- date added to LUP
- 2016-04-01 13:19:55
- date last changed
- 2022-04-14 00:36:00
@article{21f31a83-7c7d-4b79-892b-2e06fc34f0cf,
abstract = {{With increasing resistance development against conventional antibiotics, there is an urgent need to identify novel approaches for infection treatment. Antimicrobial peptides may offer opportunities in this context, hence there has been considerable interest in identification and optimization of such peptides during the last decade in particular, with the long-term aim of developing these to potent and safe therapeutics. In the present overview, focus is placed on hydrophobic modifications of antimicrobial peptides, and how these may provide opportunities to combat also more demanding pathogens, including multi-resistant strains, yet not provoking unacceptable toxic responses. In doing so, physicochemical factors affecting peptide interactions with bacterial and eukaryotic cell membranes are discussed. Throughout, an attempt is made to illustrate how physicochemical studies on model lipid membranes can be correlated to result from bacterial and cell assays, and knowledge from this translated into therapeutic considerations.}},
author = {{Schmidtchen, Artur and Pasupuleti, Mukesh and Malmsten, Martin}},
issn = {{1873-3727}},
language = {{eng}},
month = {{07}},
publisher = {{Elsevier}},
series = {{Advances in Colloid and Interface Science}},
title = {{Effect of hydrophobic modifications in antimicrobial peptides.}},
url = {{https://lup.lub.lu.se/search/files/3306795/4436186.pdf}},
doi = {{10.1016/j.cis.2013.06.009}},
year = {{2013}},
}