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Interactions between charged polypeptides and nonionic surfactants

Sjögren, Helen LU ; Ericsson, Caroline LU ; Evenas, J and Ulvenlund, Stefan LU (2005) In Biophysical Journal 89(6). p.4219-4233
Abstract
The influence of molecular characteristics on the mutual interaction between peptides and nonionic surfactants has been investigated by studying the effects of surfactants on amphiphilic, random copolymers of alpha-L-amino acids containing lysine residues as the hydrophilic parts. The hydrophobic residues were either phenylalanine or tyrosine. The peptide-surfactant interactions were studied by means of circular dichroism spectroscopy and binding isotherms, as well as by 1D and 2D NMR. The binding of surfactant to the peptides was found to be a cooperative process, appearing at surfactant concentrations just below the critical micellar concentration. However, a certain degree of peptide hydrophobicity is necessary to obtain an interaction... (More)
The influence of molecular characteristics on the mutual interaction between peptides and nonionic surfactants has been investigated by studying the effects of surfactants on amphiphilic, random copolymers of alpha-L-amino acids containing lysine residues as the hydrophilic parts. The hydrophobic residues were either phenylalanine or tyrosine. The peptide-surfactant interactions were studied by means of circular dichroism spectroscopy and binding isotherms, as well as by 1D and 2D NMR. The binding of surfactant to the peptides was found to be a cooperative process, appearing at surfactant concentrations just below the critical micellar concentration. However, a certain degree of peptide hydrophobicity is necessary to obtain an interaction with nonionic surfactant. When this prerequisite is fulfilled, the peptide mainly interacts with self-assembled, micelle-like surfactant aggregates formed onto the peptide chain. Therefore, the peptide-surfactant complex is best described in terms of a necklace model, with the peptide interacting primarily with the palisade region of the micelles via its hydrophobic side chains. The interaction yields an increased amount of alpha-helix conformation in the peptide. Surfactants that combine small headgroups with a propensity to form small, nearly spherical micelles were shown to give the largest increase in alpha-helix content. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Journal
volume
89
issue
6
pages
4219 - 4233
publisher
Cell Press
external identifiers
  • pmid:16199501
  • wos:000233590800059
  • scopus:28444449525
ISSN
1542-0086
DOI
10.1529/biophysj.105.065342
language
English
LU publication?
yes
id
c027350a-60ad-4943-8963-5a13b929d51c (old id 157596)
date added to LUP
2007-07-12 11:39:21
date last changed
2017-09-10 03:42:34
@article{c027350a-60ad-4943-8963-5a13b929d51c,
  abstract     = {The influence of molecular characteristics on the mutual interaction between peptides and nonionic surfactants has been investigated by studying the effects of surfactants on amphiphilic, random copolymers of alpha-L-amino acids containing lysine residues as the hydrophilic parts. The hydrophobic residues were either phenylalanine or tyrosine. The peptide-surfactant interactions were studied by means of circular dichroism spectroscopy and binding isotherms, as well as by 1D and 2D NMR. The binding of surfactant to the peptides was found to be a cooperative process, appearing at surfactant concentrations just below the critical micellar concentration. However, a certain degree of peptide hydrophobicity is necessary to obtain an interaction with nonionic surfactant. When this prerequisite is fulfilled, the peptide mainly interacts with self-assembled, micelle-like surfactant aggregates formed onto the peptide chain. Therefore, the peptide-surfactant complex is best described in terms of a necklace model, with the peptide interacting primarily with the palisade region of the micelles via its hydrophobic side chains. The interaction yields an increased amount of alpha-helix conformation in the peptide. Surfactants that combine small headgroups with a propensity to form small, nearly spherical micelles were shown to give the largest increase in alpha-helix content.},
  author       = {Sjögren, Helen and Ericsson, Caroline and Evenas, J and Ulvenlund, Stefan},
  issn         = {1542-0086},
  language     = {eng},
  number       = {6},
  pages        = {4219--4233},
  publisher    = {Cell Press},
  series       = {Biophysical Journal},
  title        = {Interactions between charged polypeptides and nonionic surfactants},
  url          = {http://dx.doi.org/10.1529/biophysj.105.065342},
  volume       = {89},
  year         = {2005},
}