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

Emma Sparr1, Dragomir N Ganchev, Margot M E Snel

  • 1Department of Biochemistry of Membranes, Institute of Biomembranes, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands. emma.sparr@fkem1.lu.se

Biochemistry
|January 5, 2005
PubMed

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.

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