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Title: Conformation of ceramide 6 molecules and chain-flip transitions in the lipid matrix of the outermost layer of mammalian skin, the stratum corneum

Abstract

Neutron diffraction from oriented multilamellar model stratum corneum (SC) membranes provides information on the internal nanostructure and hydration of the lipid bilayer. The main distinguishing feature of model SC membranes based on ceramide 6 is the extremely small intermembrane space (1 A). The role of the fully extended (FE) conformation of ceramide 6 molecules in the organization of the nanostructure of the lipid matrix is discussed. The FE conformation gives rise to extremely strong intermembrane attractions (armature reinforcement), which tighten the adjacent bilayers to form steric contacts. Chain-flip transitions in the conformation of ceramide molecules account for structural alterations in native and model SC membranes upon their hydration.

Authors:
 [1]
  1. Joint Institute for Nuclear Research (Russian Federation), E-mail: kiselev@jinr.ru
Publication Date:
OSTI Identifier:
21090902
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 52; Journal Issue: 3; Other Information: DOI: 10.1134/S1063774507030340; Copyright (c) 2007 Nauka/Interperiodica; Article Copyright (c) 2007 Pleiades Publishing, Inc; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; HYDRATION; LAYERS; LIPIDS; MEMBRANES; NANOSTRUCTURES; NEUTRON DIFFRACTION; SKIN

Citation Formats

Kiselev, M. A. Conformation of ceramide 6 molecules and chain-flip transitions in the lipid matrix of the outermost layer of mammalian skin, the stratum corneum. United States: N. p., 2007. Web. doi:10.1134/S1063774507030340.
Kiselev, M. A. Conformation of ceramide 6 molecules and chain-flip transitions in the lipid matrix of the outermost layer of mammalian skin, the stratum corneum. United States. doi:10.1134/S1063774507030340.
Kiselev, M. A. Tue . "Conformation of ceramide 6 molecules and chain-flip transitions in the lipid matrix of the outermost layer of mammalian skin, the stratum corneum". United States. doi:10.1134/S1063774507030340.
@article{osti_21090902,
title = {Conformation of ceramide 6 molecules and chain-flip transitions in the lipid matrix of the outermost layer of mammalian skin, the stratum corneum},
author = {Kiselev, M. A.},
abstractNote = {Neutron diffraction from oriented multilamellar model stratum corneum (SC) membranes provides information on the internal nanostructure and hydration of the lipid bilayer. The main distinguishing feature of model SC membranes based on ceramide 6 is the extremely small intermembrane space (1 A). The role of the fully extended (FE) conformation of ceramide 6 molecules in the organization of the nanostructure of the lipid matrix is discussed. The FE conformation gives rise to extremely strong intermembrane attractions (armature reinforcement), which tighten the adjacent bilayers to form steric contacts. Chain-flip transitions in the conformation of ceramide molecules account for structural alterations in native and model SC membranes upon their hydration.},
doi = {10.1134/S1063774507030340},
journal = {Crystallography Reports},
number = 3,
volume = 52,
place = {United States},
year = {Tue May 15 00:00:00 EDT 2007},
month = {Tue May 15 00:00:00 EDT 2007}
}
  • The stratum corneum is the uppermost layer of the skin and acts as a barrier to keep out contaminants and retain moisture. Understanding the molecular structure and behavior of this layer will provide guidance for optimizing its biological function. In this study we use a model mixture comprised of equimolar portions of ceramide NS (24:0), lignoceric acid, and cholesterol to model the effect of the addition of small amounts of oleic acid to the bilayer at 300 and 340 K. Five systems at each temperature have been simulated with concentrations between 0 and 0.1 mol % oleic acid. Our majormore » finding is that subdiffusive behavior over the 200 ns time scale is evident in systems at 340 K, with cholesterol diffusion being enhanced with increased oleic acid. Importantly, cholesterol and other species diffuse faster when radial densities indicate nearest neighbors include more cholesterol. We also find that, with the addition of oleic acid, the bilayer midplane and interfacial densities are reduced and there is a 3% decrease in total thickness occurring mostly near the hydrophilic interface at 300 K with reduced overall density at 340 K. Increased interdigitation occurs independent of oleic acid with a temperature increase. Slight ordering of the long non-hydroxy fatty acid of the ceramide occurs near the hydrophilic interface as a function of the oleic acid concentration, but no significant impact on hydrogen bonding is seen in the chosen oleic acid concentrations.« less
  • The lipid of the outermost layer of the skin is confined largely to the extracellular spaces surrounding the corneocytes of the stratum corneum where it forms a multilamellar adhesive matrix to act as the major permeability barrier of the skin. Knowledge of the molecular architecture of these intercellular domains is important for understanding various skin pathologies and their treatment, percutaneous drug delivery, and the cosmetic maintenance of the skin. The authors have surveyed by X-ray diffraction the structure of the intercellular domains and the extracted lipids of murine stratum corneum (SC) at 25, 45, and 70/sup 0/C which are temperaturesmore » in the vicinity of known thermal phase transitions. The intercellular domains produce lamellar diffraction patterns with a Bragg spacing of 131 +/- 2 A. Lipid extracted from the SC and dispersed in excess water does not produce a simple lamellar diffraction pattern at any temperature studied, however. This and other facts suggest that another component, probably a protein, must be present to control the architecture of the intercellular lipid domains. They have also obtained diffraction patterns attributable to the protein envelopes of the corneocytes. The patterns suggest a ..beta..-pleated sheet organizational scheme. No diffraction patterns were observed that could be attributed to keratin.« less