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Molecular organization in striated domains induced by transmembrane alpha-helical peptides in dipalmitoyl phosphatidylcholine bilayers

Sparr, Emma LU ; Ganchev, D N; Snel, M M E; Ridder, Anja; Kroon-Batenburg, L M J; Chupin, V; Rijkers, D T S; Killian, J A and de Kruijff, B (2005) In Biochemistry 44(1). p.2-10
Abstract
Transmembrane (TM) alpha-helical peptides with neutral flanking residues such as tryptophan form highly ordered striated domains when incorporated in gel-state 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) bilayers and inspected by atomic force microscopy (AFM) (1). In this study, we analyze the molecular organization of these striated domains using AFM, photo-cross-linking, fluorescence spectroscopy, nuclear magnetic resonance (NMR), and X-ray diffraction techniques on different functionalized TM peptides. The results demonstrate that the striated domains consist of linear arrays of single TM peptides with a dominantly antiparallel organization in which the peptides interact with each other and with lipids. The peptide arrays are... (More)
Transmembrane (TM) alpha-helical peptides with neutral flanking residues such as tryptophan form highly ordered striated domains when incorporated in gel-state 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) bilayers and inspected by atomic force microscopy (AFM) (1). In this study, we analyze the molecular organization of these striated domains using AFM, photo-cross-linking, fluorescence spectroscopy, nuclear magnetic resonance (NMR), and X-ray diffraction techniques on different functionalized TM peptides. The results demonstrate that the striated domains consist of linear arrays of single TM peptides with a dominantly antiparallel organization in which the peptides interact with each other and with lipids. The peptide arrays are regularly spaced by +/-8.5 nm and are separated by somewhat perturbed gel-state lipids with hexagonally organized acyl chains, which have lost their tilt. This system provides an example of how domains of peptides and lipids can be formed in membranes as a result of a combination of specific peptide-peptide and peptide-lipid interactions. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
44
issue
1
pages
2 - 10
publisher
The American Chemical Society
external identifiers
  • wos:000226214600002
  • pmid:15628840
  • scopus:11844265875
ISSN
0006-2960
DOI
10.1021/bi048047a
language
English
LU publication?
yes
id
74787880-e2f5-479f-91b0-c2f46452ec5d (old id 157620)
date added to LUP
2007-07-12 11:50:21
date last changed
2017-01-01 04:27:34
@article{74787880-e2f5-479f-91b0-c2f46452ec5d,
  abstract     = {Transmembrane (TM) alpha-helical peptides with neutral flanking residues such as tryptophan form highly ordered striated domains when incorporated in gel-state 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) bilayers and inspected by atomic force microscopy (AFM) (1). In this study, we analyze the molecular organization of these striated domains using AFM, photo-cross-linking, fluorescence spectroscopy, nuclear magnetic resonance (NMR), and X-ray diffraction techniques on different functionalized TM peptides. The results demonstrate that the striated domains consist of linear arrays of single TM peptides with a dominantly antiparallel organization in which the peptides interact with each other and with lipids. The peptide arrays are regularly spaced by +/-8.5 nm and are separated by somewhat perturbed gel-state lipids with hexagonally organized acyl chains, which have lost their tilt. This system provides an example of how domains of peptides and lipids can be formed in membranes as a result of a combination of specific peptide-peptide and peptide-lipid interactions.},
  author       = {Sparr, Emma and Ganchev, D N and Snel, M M E and Ridder, Anja and Kroon-Batenburg, L M J and Chupin, V and Rijkers, D T S and Killian, J A and de Kruijff, B},
  issn         = {0006-2960},
  language     = {eng},
  number       = {1},
  pages        = {2--10},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Molecular organization in striated domains induced by transmembrane alpha-helical peptides in dipalmitoyl phosphatidylcholine bilayers},
  url          = {http://dx.doi.org/10.1021/bi048047a},
  volume       = {44},
  year         = {2005},
}