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Bactericidal and hemolytic properties of mixed LL-37/surfactant systems

Reijmar, K.; Schmidtchen, Artur LU and Malmsten, M. (2007) In Journal of Drug Delivery Science and Technology 17(4). p.293-297
Abstract
The interaction between acyl chain homologues (C10 and C12) of n-acyl beta-D-maltoside and the antimicrobial peptide LL-37 (LLGDFFRK-SKEKIGKEFKRIVQRIKDFLRNLVPRTES) was investigated. Emphasis was placed on peptide-micelle complexation and its consequences for peptide proteolytic stability, as well as bactericidal and hemolytic effects of the mixed systems. From circular dichroism and liposome leakage experiments, it was found that LL-37 interacts with both surfactants investigated, and that this reduces the effective free peptide concentration. Analogously, LL-37 displayed increased proteolytic stability towards Pseudomonas aeruginosa elastase in surfactant solution. Despite this, conditions can be found at which the bactericidal effect of... (More)
The interaction between acyl chain homologues (C10 and C12) of n-acyl beta-D-maltoside and the antimicrobial peptide LL-37 (LLGDFFRK-SKEKIGKEFKRIVQRIKDFLRNLVPRTES) was investigated. Emphasis was placed on peptide-micelle complexation and its consequences for peptide proteolytic stability, as well as bactericidal and hemolytic effects of the mixed systems. From circular dichroism and liposome leakage experiments, it was found that LL-37 interacts with both surfactants investigated, and that this reduces the effective free peptide concentration. Analogously, LL-37 displayed increased proteolytic stability towards Pseudomonas aeruginosa elastase in surfactant solution. Despite this, conditions can be found at which the bactericidal effect of mixed peptide-surfactant systems is comparable to that of free LL-37. However also a number of challenges to this type of antimicrobial peptide (AMP) carrier system were identified, notably related to reduction of bactericidal effect for some systems, and occurrence of hemolysis for mixed peptide-surfactant systems displaying advantageous bactericidal effects. Any use of such AMP carrier systems will therefore have to be carefully optimized in order to retain bactericidal activity and minimize toxicity. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
maltoside, LL-37, hemolysis, antimicrobial, bacteria, micelle, surfactant
in
Journal of Drug Delivery Science and Technology
volume
17
issue
4
pages
293 - 297
publisher
EDITIONS SANTE
external identifiers
  • wos:000250032200010
  • scopus:34548580963
ISSN
1773-2247
language
English
LU publication?
yes
id
cb6378eb-8f95-4b58-bec9-7f0e67190d23 (old id 655194)
date added to LUP
2007-12-14 10:56:24
date last changed
2017-01-01 07:18:19
@article{cb6378eb-8f95-4b58-bec9-7f0e67190d23,
  abstract     = {The interaction between acyl chain homologues (C10 and C12) of n-acyl beta-D-maltoside and the antimicrobial peptide LL-37 (LLGDFFRK-SKEKIGKEFKRIVQRIKDFLRNLVPRTES) was investigated. Emphasis was placed on peptide-micelle complexation and its consequences for peptide proteolytic stability, as well as bactericidal and hemolytic effects of the mixed systems. From circular dichroism and liposome leakage experiments, it was found that LL-37 interacts with both surfactants investigated, and that this reduces the effective free peptide concentration. Analogously, LL-37 displayed increased proteolytic stability towards Pseudomonas aeruginosa elastase in surfactant solution. Despite this, conditions can be found at which the bactericidal effect of mixed peptide-surfactant systems is comparable to that of free LL-37. However also a number of challenges to this type of antimicrobial peptide (AMP) carrier system were identified, notably related to reduction of bactericidal effect for some systems, and occurrence of hemolysis for mixed peptide-surfactant systems displaying advantageous bactericidal effects. Any use of such AMP carrier systems will therefore have to be carefully optimized in order to retain bactericidal activity and minimize toxicity.},
  author       = {Reijmar, K. and Schmidtchen, Artur and Malmsten, M.},
  issn         = {1773-2247},
  keyword      = {maltoside,LL-37,hemolysis,antimicrobial,bacteria,micelle,surfactant},
  language     = {eng},
  number       = {4},
  pages        = {293--297},
  publisher    = {EDITIONS SANTE},
  series       = {Journal of Drug Delivery Science and Technology},
  title        = {Bactericidal and hemolytic properties of mixed LL-37/surfactant systems},
  volume       = {17},
  year         = {2007},
}