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Binding and Release of Consensus Peptides by Poly(acrylic acid) Microgels.

Bysell, Helena; Schmidtchen, Artur LU and Malmsten, Martin (2009) In Biomacromolecules 10. p.2162-2168
Abstract
The interaction between positively charged consensus peptides and poly(acrylic acid) microgels was investigated with micromanipulator-assisted light microscopy and confocal laser scanning microscopy. Peptide binding and release was monitored by microgel deswelling and swelling for monodisperse multiples of heparin-binding Cardin and Weintraub motifs, (AKKARA)(n) (1 </= n </= 4) and (ARKKAAKA)(n) (1 </= n </= 3), as well as the corresponding titratable (AHHAHA)(4) and (AHHHAAHA)(3) peptides (A, K, R and H, refering to alanine, lysine, arginine, and histidine, respectively). When fully charged, these peptides distribute homogenously throughout the microgels and display concentration-dependent deswelling, which increases with... (More)
The interaction between positively charged consensus peptides and poly(acrylic acid) microgels was investigated with micromanipulator-assisted light microscopy and confocal laser scanning microscopy. Peptide binding and release was monitored by microgel deswelling and swelling for monodisperse multiples of heparin-binding Cardin and Weintraub motifs, (AKKARA)(n) (1 </= n </= 4) and (ARKKAAKA)(n) (1 </= n </= 3), as well as the corresponding titratable (AHHAHA)(4) and (AHHHAAHA)(3) peptides (A, K, R and H, refering to alanine, lysine, arginine, and histidine, respectively). When fully charged, these peptides distribute homogenously throughout the microgels and display concentration-dependent deswelling, which increases with increasing peptide length. Both (AKKARA)(4) and (ARKKAAKA)(3) display potent and fast microgel deswelling but only marginal subsequent electrolyte-induced desorption. In contrast, reducing the peptide charge for (AHHAHA)(4) and (AHHHAAHA)(3) at neutral and high pH, or the peptide length, substantially reduces the peptide affinity for the microgels and facilitates rapid peptide release. Taken together, the results also show that quite short peptides of moderate charge density interact strongly and cause extensive gel deswelling of oppositely charged microgels, precluding peptide release. They also show, however, that desirable triggered release can be achieved with peptides of lower charge density. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
10
pages
2162 - 2168
publisher
The American Chemical Society
external identifiers
  • wos:000268661400017
  • pmid:19583241
  • scopus:68849108390
ISSN
1526-4602
DOI
10.1021/bm9003354
language
English
LU publication?
yes
id
8de3f81a-95fa-4839-8293-d65574f27a51 (old id 1453331)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19583241?dopt=Abstract
date added to LUP
2009-08-04 10:12:57
date last changed
2017-12-10 04:43:34
@article{8de3f81a-95fa-4839-8293-d65574f27a51,
  abstract     = {The interaction between positively charged consensus peptides and poly(acrylic acid) microgels was investigated with micromanipulator-assisted light microscopy and confocal laser scanning microscopy. Peptide binding and release was monitored by microgel deswelling and swelling for monodisperse multiples of heparin-binding Cardin and Weintraub motifs, (AKKARA)(n) (1 &lt;/= n &lt;/= 4) and (ARKKAAKA)(n) (1 &lt;/= n &lt;/= 3), as well as the corresponding titratable (AHHAHA)(4) and (AHHHAAHA)(3) peptides (A, K, R and H, refering to alanine, lysine, arginine, and histidine, respectively). When fully charged, these peptides distribute homogenously throughout the microgels and display concentration-dependent deswelling, which increases with increasing peptide length. Both (AKKARA)(4) and (ARKKAAKA)(3) display potent and fast microgel deswelling but only marginal subsequent electrolyte-induced desorption. In contrast, reducing the peptide charge for (AHHAHA)(4) and (AHHHAAHA)(3) at neutral and high pH, or the peptide length, substantially reduces the peptide affinity for the microgels and facilitates rapid peptide release. Taken together, the results also show that quite short peptides of moderate charge density interact strongly and cause extensive gel deswelling of oppositely charged microgels, precluding peptide release. They also show, however, that desirable triggered release can be achieved with peptides of lower charge density.},
  author       = {Bysell, Helena and Schmidtchen, Artur and Malmsten, Martin},
  issn         = {1526-4602},
  language     = {eng},
  pages        = {2162--2168},
  publisher    = {The American Chemical Society},
  series       = {Biomacromolecules},
  title        = {Binding and Release of Consensus Peptides by Poly(acrylic acid) Microgels.},
  url          = {http://dx.doi.org/10.1021/bm9003354},
  volume       = {10},
  year         = {2009},
}