Effects of Peptide Secondary Structure on the Interaction with Oppositely Charged Microgels.
(2011) In Biomacromolecules 12. p.419-424- Abstract
- The importance of peptide secondary structure on the interaction between antimicrobial peptides and oppositely charged poly(acrylic acid-co-acrylamide) microgels of various charge density was investigated for EFKRIVQRIKDFLRNLV (EFK17). Through d-enantiomer (EFK17-d/a; E(dF)KR(dI)VQR(dI)KD(dF)LRNLV) or tryptophan (EFK17-W/a; EWKRWVQRWKDFLRNLV) substitutions, both conformation-dependent and -independent amphiphilicity of this peptide could be precisely controlled. Peptide secondary structure was investigated by circular dichroism, whereas microgel deswelling and reswelling in response to peptide binding and release were studied by micromanipulator-assisted light and fluorescence microscopy, and peptide uptake in the microgels was determined... (More)
- The importance of peptide secondary structure on the interaction between antimicrobial peptides and oppositely charged poly(acrylic acid-co-acrylamide) microgels of various charge density was investigated for EFKRIVQRIKDFLRNLV (EFK17). Through d-enantiomer (EFK17-d/a; E(dF)KR(dI)VQR(dI)KD(dF)LRNLV) or tryptophan (EFK17-W/a; EWKRWVQRWKDFLRNLV) substitutions, both conformation-dependent and -independent amphiphilicity of this peptide could be precisely controlled. Peptide secondary structure was investigated by circular dichroism, whereas microgel deswelling and reswelling in response to peptide binding and release were studied by micromanipulator-assisted light and fluorescence microscopy, and peptide uptake in the microgels was determined from solution depletion measurements. Results show that peptide binding to the microgel is highly influenced by peptide secondary structure. EFK17-a, characterized by an idealized helix with all polar/charged amino acids located at one side of the helix, and all nonpolar/hydrophobic residues on the other, displays pronounced α-helix induction on peptide binding to the microgels. EFK17-d/a, on the other hand, displays no such amphiphilic helix induction. Mirroring this, EFK17-a displays substantially higher binding to the microgels than EFK17-d/a as well as much larger peptide-induced microgel deswelling. For EFK17-W/a, both conformation-dependent and -independent amphiphilicity effects were demonstrated. Overall, the results show that peptide conformational aspects need to be considered in peptide/microgel interactions, for example, in the design of microgel carrier systems for peptide drugs. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1755828
- author
- Månsson, Ronja ; Bysell, Helena ; Hansson, Per ; Schmidtchen, Artur LU and Malmsten, Martin LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biomacromolecules
- volume
- 12
- pages
- 419 - 424
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000287175700017
- pmid:21182237
- scopus:79951643215
- pmid:21182237
- ISSN
- 1526-4602
- DOI
- 10.1021/bm101165e
- language
- English
- LU publication?
- yes
- id
- 045f8a71-76ef-4500-82ff-985c558dec36 (old id 1755828)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21182237?dopt=Abstract
- date added to LUP
- 2016-04-04 07:07:02
- date last changed
- 2022-02-20 19:52:35
@article{045f8a71-76ef-4500-82ff-985c558dec36,
abstract = {{The importance of peptide secondary structure on the interaction between antimicrobial peptides and oppositely charged poly(acrylic acid-co-acrylamide) microgels of various charge density was investigated for EFKRIVQRIKDFLRNLV (EFK17). Through d-enantiomer (EFK17-d/a; E(dF)KR(dI)VQR(dI)KD(dF)LRNLV) or tryptophan (EFK17-W/a; EWKRWVQRWKDFLRNLV) substitutions, both conformation-dependent and -independent amphiphilicity of this peptide could be precisely controlled. Peptide secondary structure was investigated by circular dichroism, whereas microgel deswelling and reswelling in response to peptide binding and release were studied by micromanipulator-assisted light and fluorescence microscopy, and peptide uptake in the microgels was determined from solution depletion measurements. Results show that peptide binding to the microgel is highly influenced by peptide secondary structure. EFK17-a, characterized by an idealized helix with all polar/charged amino acids located at one side of the helix, and all nonpolar/hydrophobic residues on the other, displays pronounced α-helix induction on peptide binding to the microgels. EFK17-d/a, on the other hand, displays no such amphiphilic helix induction. Mirroring this, EFK17-a displays substantially higher binding to the microgels than EFK17-d/a as well as much larger peptide-induced microgel deswelling. For EFK17-W/a, both conformation-dependent and -independent amphiphilicity effects were demonstrated. Overall, the results show that peptide conformational aspects need to be considered in peptide/microgel interactions, for example, in the design of microgel carrier systems for peptide drugs.}},
author = {{Månsson, Ronja and Bysell, Helena and Hansson, Per and Schmidtchen, Artur and Malmsten, Martin}},
issn = {{1526-4602}},
language = {{eng}},
pages = {{419--424}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biomacromolecules}},
title = {{Effects of Peptide Secondary Structure on the Interaction with Oppositely Charged Microgels.}},
url = {{http://dx.doi.org/10.1021/bm101165e}},
doi = {{10.1021/bm101165e}},
volume = {{12}},
year = {{2011}},
}