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Effect of Hydrophobicity on the Interaction between Antimicrobial Peptides and Poly(acrylic acid) Microgels

Bysell, Helena; Ransson, Per; Schmidtchen, Artur LU and Malmsten, Martin (2010) In The Journal of Physical Chemistry Part B 114(3). p.1307-1313
Abstract
The influence of peptide hydrophobicity on the interaction between antimicrobial peptides and poly(acrylic, acid) microgels wits studied by end-tagging the kininogen-derived antimicrobial peptide GKHKNKGKKNGKHNGWK (GKH17) and its truncated variant KNKGKKNGKH (KNK10) with oligotryptophan groups of different lengths. Microgel deswelling and reswelling in response to peptide binding and release was studied by micromanipulator-assisted light- and fluorescence microscopy, peptide uptake in microgels was determined from solution depletion measurements, and peptide oligomerization was monitored by fluorescence spectroscopy. Results showed that oligomerizition/aggregation of the hydrophobically end-tagged peptides is either absent or characterized... (More)
The influence of peptide hydrophobicity on the interaction between antimicrobial peptides and poly(acrylic, acid) microgels wits studied by end-tagging the kininogen-derived antimicrobial peptide GKHKNKGKKNGKHNGWK (GKH17) and its truncated variant KNKGKKNGKH (KNK10) with oligotryptophan groups of different lengths. Microgel deswelling and reswelling in response to peptide binding and release was studied by micromanipulator-assisted light- and fluorescence microscopy, peptide uptake in microgels was determined from solution depletion measurements, and peptide oligomerization was monitored by fluorescence spectroscopy. Results showed that oligomerizition/aggregation of the hydrophobically end-tagged peptides is either absent or characterized by exposure of the tryptophan residues to the aqueous ambient, the latter suggesting small aggregation numbers. In addition, peptide uptake and affinity to the poly(acrylic acid) microgels increase with the number of trypthophan residues in the hydrophobic end tag, whereas peptide-induced microgel deswelling kinetics did not display this tag-length dependence to the same extent. Instead, long end tags resulted in anomalous shell formation, opposing further peptide-induced network deswelling. Theoretical modeling suggested that the deswelling kinetics in response to peptide binding is largely controlled by stagnant layer diffusion, but also that for peptides with Sufficiently long hydrophobic tags, the shell constitutes an additional diffusion barrier, thus resulting in slower microgel deswelling. In addition, GKH17 and KNK10 peptides lacking the tryptophan end tags were Substantially released on reducing peptide-microgel electrostatic interactions through addition of salt, an effect more pronounced for the shorter KNK10 peptide, whereas the hydrophobically end-tagged peptides remained bound to the microgels also at high ionic strength. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
114
issue
3
pages
1307 - 1313
publisher
The American Chemical Society
external identifiers
  • wos:000273672300012
  • scopus:76249113063
ISSN
1520-5207
DOI
10.1021/jp910068t
language
English
LU publication?
yes
id
cdc9c295-bdca-4bf5-a514-551aced30d7c (old id 1547483)
date added to LUP
2010-02-23 14:39:53
date last changed
2018-05-29 10:52:17
@article{cdc9c295-bdca-4bf5-a514-551aced30d7c,
  abstract     = {The influence of peptide hydrophobicity on the interaction between antimicrobial peptides and poly(acrylic, acid) microgels wits studied by end-tagging the kininogen-derived antimicrobial peptide GKHKNKGKKNGKHNGWK (GKH17) and its truncated variant KNKGKKNGKH (KNK10) with oligotryptophan groups of different lengths. Microgel deswelling and reswelling in response to peptide binding and release was studied by micromanipulator-assisted light- and fluorescence microscopy, peptide uptake in microgels was determined from solution depletion measurements, and peptide oligomerization was monitored by fluorescence spectroscopy. Results showed that oligomerizition/aggregation of the hydrophobically end-tagged peptides is either absent or characterized by exposure of the tryptophan residues to the aqueous ambient, the latter suggesting small aggregation numbers. In addition, peptide uptake and affinity to the poly(acrylic acid) microgels increase with the number of trypthophan residues in the hydrophobic end tag, whereas peptide-induced microgel deswelling kinetics did not display this tag-length dependence to the same extent. Instead, long end tags resulted in anomalous shell formation, opposing further peptide-induced network deswelling. Theoretical modeling suggested that the deswelling kinetics in response to peptide binding is largely controlled by stagnant layer diffusion, but also that for peptides with Sufficiently long hydrophobic tags, the shell constitutes an additional diffusion barrier, thus resulting in slower microgel deswelling. In addition, GKH17 and KNK10 peptides lacking the tryptophan end tags were Substantially released on reducing peptide-microgel electrostatic interactions through addition of salt, an effect more pronounced for the shorter KNK10 peptide, whereas the hydrophobically end-tagged peptides remained bound to the microgels also at high ionic strength.},
  author       = {Bysell, Helena and Ransson, Per and Schmidtchen, Artur and Malmsten, Martin},
  issn         = {1520-5207},
  language     = {eng},
  number       = {3},
  pages        = {1307--1313},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Effect of Hydrophobicity on the Interaction between Antimicrobial Peptides and Poly(acrylic acid) Microgels},
  url          = {http://dx.doi.org/10.1021/jp910068t},
  volume       = {114},
  year         = {2010},
}