Molecular organization in striated domains induced by transmembrane alpha-helical peptides in dipalmitoyl phosphatidylcholine bilayers
(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:
https://lup.lub.lu.se/record/157620
- author
- 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
- organization
- publishing date
- 2005
- 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}}, }