Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; and
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 (ACS)
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
2016-04-01 11:42:14
date last changed
2022-01-26 17:00:38
@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 (ACS)}},
  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}},
  doi          = {{10.1021/bi048047a}},
  volume       = {{44}},
  year         = {{2005}},
}