About: Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering

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About: Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering
Creator	Beerlink, André Diederichsen, Ulf Salditt, Tim Salditt, Á Schneggenburger, Philipp Weinhausen, Britta Beerlink, A Diederichsen, U Diederichsen, Á Schneggenburger, P Weinhausen, Á
source	PMC
abstract	Studying membrane active peptides or protein fragments within the lipid bilayer environment is particularly challenging in the case of synthetically modified, labeled, artificial, or recently discovered native structures. For such samples the localization and orientation of the molecular species or probe within the lipid bilayer environment is the focus of research prior to an evaluation of their dynamic or mechanistic behavior. X-ray scattering is a powerful method to study peptide/lipid interactions in the fluid, fully hydrated state of a lipid bilayer. For one, the lipid response can be revealed by observing membrane thickening and thinning as well as packing in the membrane plane; at the same time, the distinct positions of peptide moieties within lipid membranes can be elucidated at resolutions of up to several angstroms by applying heavy-atom labeling techniques. In this study, we describe a generally applicable X-ray scattering approach that provides robust and quantitative information about peptide insertion and localization as well as peptide/lipid interaction within highly oriented, hydrated multilamellar membrane stacks. To this end, we have studied an artificial, designed β-helical peptide motif in its homodimeric and hairpin variants adopting different states of oligomerization. These peptide lipid complexes were analyzed by grazing incidence diffraction (GID) to monitor changes in the lateral lipid packing and ordering. In addition, we have applied anomalous reflectivity using synchrotron radiation as well as in-house X-ray reflectivity in combination with iodine-labeling in order to determine the electron density distribution ρ(z) along the membrane normal (z axis), and thereby reveal the hydrophobic mismatch situation as well as the position of certain amino acid side chains within the lipid bilayer. In the case of multiple labeling, the latter technique is not only applicable to demonstrate the peptide’s reconstitution but also to generate evidence about the relative peptide orientation with respect to the lipid bilayer. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00249-010-0645-4) contains supplementary material, which is available to authorized users.
has issue date	2010-12-23(xsd:dateTime)
bibo:doi	10.1007/s00249-010-0645-4
bibo:pmid	21181143
has license	cc-by-nc
sha1sum (hex)	5e1017f2def4ac50f1b63bd52a9a2214c1dfd3b7
schema:url	https://doi.org/10.1007/s00249-010-0645-4
resource representing a document's title	Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering
has PubMed Central identifier	PMC3070074
has PubMed identifier	21181143
schema:publication	Eur Biophys J
resource representing a document's body	covid:5e1017f2def4ac50f1b63bd52a9a2214c1dfd3b7#body_text
is schema:about of	named entity 'lipid' named entity 'X-ray scattering' named entity 'RSM' named entity '455th' named entity 'chain' named entity 'AMP' named entity 'active' named entity 'lipid' named entity 'X-ray scattering' named entity 'model' named entity 'helices' named entity 'lipid' named entity 'Reciprocal space' named entity 'FRET' named entity 'Relative humidity' named entity 'phosphocholine' named entity 'X-ray scattering' named entity 'lipid membranes' named entity 'Küsel' named entity 'acyl chains' named entity 'electron density' named entity 'hydrophobic' named entity 'aromatic' named entity 'one-dimensional' named entity 'peptide' named entity 'Gly' named entity 'acyl chains' named entity 'multilamellar' named entity 'Lys' named entity 'Gly' named entity 'Phe' named entity 'GID' named entity 'peptide' named entity 'X-ray reflectivity' named entity 'lipid bilayer' named entity 'relative humidity' named entity 'headgroup' named entity 'Küsel' named entity 'homodimer' named entity 'headgroup' named entity 'order parameters' named entity 'multilamellar' named entity 'dimer' named entity 'oligomerization' named entity 'red arrows' named entity 'PNA' named entity 'lipid' named entity 'electron paramagnetic resonance' named entity 'lipid' named entity 'iodine' named entity 'peptide' named entity 'mass flow' named entity 'Phe' named entity 'real space' named entity 'GID' named entity 'membrane surface' named entity 'GISAXS' named entity 'electron density' named entity 'peptide' named entity 'peptide' named entity 'molecular species' named entity 'GID' named entity 'lipid' named entity 'analytical method' named entity 'elasticity' named entity 'lipid bilayer' named entity 'condensed phase' named entity 'helix' named entity 'electron density' named entity 'peptide' named entity 'Küsel'

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