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W Bras

Publications and source records attributed to W Bras.

25 records · Page 2Linked to original sources
PubMed1994

The lipid and protein structure of mouse stratum corneum: a wide and small angle diffraction study.

The structure of mouse stratum corneum was investigated using small and wide angle X-ray scattering. Diffraction patterns were collected as a function of temperature and hydration. The lipid lamellar structure is characterized by a repeat distance of 13.4 nm. Occasionally a second lipid lamellar phase has been found with a repeat distance of 6.1 nm. Upon hydration neither swelling of the lamellae nor lateral swelling of the lipids was found. On the basis of these facts it was concluded that the size of the crystallographic unit cell of the lipid structure is insensitive to the water content. The 13.4 nm lamellar phase disappeared upon heating to 55 degrees C. At 45 degrees C the orthorhombic lateral packing disappeared. At this temperature only an hexagonal and liquid lateral packing of the lipids was observed. The hexagonal lateral packing transformed to a liquid one between 45 degrees C and 80 degrees C. Model calculations were carried out to obtain the electron density profile of the lamellar structure. In all models three electron lucent regions were fitted between which electron dense regions are located indicating that the 13.4 nm lamellar structure consist of three bilayers.

Animals↗
PubMed1994

Synchrotron X-ray studies of lipids and membranes: a critique.

This review gives a description of techniques, suitable for the study of lipid dispersions and unorientated membranes, that are available at synchrotron facilities to determine either the kinetics of transitional phenomena in the time after a temperature or pressure jump is initiated, or the phases present while a sample undergoes a phase transition. Included in this description is information about synchrotron X-ray sources, sample holders and temperature controllers, detection systems, as well as data reduction. Examples involving lipid dispersions are provided to illustrate the application of these methods using synchrotron radiation.

Kinetics↗
PubMed1993

Small angle X-ray scattering: possibilities and limitations in characterization of vesicles.

The use of small angle X-ray scattering (SAXS) for characterization of lipid vesicle dispersions is described. The effect of curvature of the membrane, the presence of proteins in the core and on the surface of the membrane, variations in membrane thickness and distribution in the number of bilayers of the vesicles in the dispersion on the scattering curve is discussed. Concerning unilamellar vesicles, either the membrane curvature of vesicles smaller than 50 nm or variations in membrane thickness result in a disappearance of the first node in the scattering curve, even if the bilayer is symmetric with respect to the electron density distribution. In the case of dispersion in which unilamellar as well as multilamellar vesicles are present it is shown that a small fraction of multilamellar liposomes changes the scattering curve dramatically. Liposomes were prepared from various compositions of dipalmitoylphosphatidylcholine (DPPC) and cholesterol hemisuccinate (CHEMS) by the film method. The electron density profile of the bilayers and distribution in the number of bilayers of the liposome dispersions were determined. The average number of bilayers increased as a function of the decrease in CHEMS content. Liposomes with higher CHEMS content than 10 mol% were unilamellar. It seems that increase in charge intercalated in the bilayers resulted in unilamellar vesicles.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1992

Tetragonal deformation of the hexagonal myofilament matrix in single skinned skeletal muscle fibres owing to change in sarcomere length.

Single skinned skeletal muscle fibres were immersed in solutions containing two different levels of activator calcium (pCa: 4.4; 6.0). Sarcomere length was varied from 1.6 to 3.5 microns and recorded by laser diffraction. Slack length was 2.0 microns. Small-angle equatorial X-ray diffraction patterns of relaxed and activated fibres at different sarcomere lengths were recorded using synchrotron radiation. The position and amplitude of the diffraction peaks were calculated from the spectra based on the hexagonal arrangement of the myofilament matrix, relating the position of the (1.0)- and (1.1)-diffraction peaks in this model by square root of 3. The diffraction peaks were fitted by five Gaussian functions (1.0, 1.1, 2.0, 2.1 and Z-line) and residual background was corrected by means of a hyperbola. The coupling of the position of the (1.0)- and (1.1)-peak was expressed as a factor: FAC = [d(1.0)/d(1.1)]/square root 3. In the relaxed state this coupling factor decreased at increasing sarcomere length (0.9880 +/- 0.002 at 2.0 microns; 0.900 +/- 0.01 at 3.5 microns). The coupling factor tends toward the one that will be obtained from the squared structure of actin filaments near the Z-discs. At shorter sarcomere lengths a decrease of the coupling factor has also been seen (0.9600 +/- 0.005 at 1.6 microns), giving rise to an increased uniform deformation of the hexagonal matrix, when sarcomere length is changed from slack length. From these experiments we conclude that a change in sarcomere length (from slack length) increases the deformation of the actin-myosin matrix to a tetragonal lattice.

Actin Cytoskeleton↗
PubMed1991

Structural investigations of human stratum corneum by small-angle X-ray scattering.

The structure of human stratum corneum was investigated with small-angle X-ray scattering (SAXS). At room temperature the scattering curve was characterized by a strong intensity at low scattering vector (Q less than 0.8 nm-1) and two complicated diffraction peaks originating from a lamellar structure of the lipids. The lamellar lipid structure in the stratum corneum transformed to a disordered structure between 65 degrees C and 75 degrees C, the same temperature region at which a thermal lipid transition occurred. After cooling down to room temperature a recrystallization of at least a part of the lipids took place, after which only one unit cell with a repeat distance of 13.4 nm could be detected. Comparison of the scattering curve of the stratum corneum after crystallization with the scattering curve of the stratum corneum before recrystallization leads to the conclusion that in the original curve the lipids are arranged in two unit cells with repeat distances of 6.4 nm and 13.4 nm. From model calculations it appears that the latter unit cell consists of more than one bilayer. The scattering curves of stratum corneum hydrated to various levels were measured. A change in the water content of stratum corneum between 6% w/w and 60% w/w (fully hydrated) did not result in swelling of the bilayers, but the scattering curve obtained with stratum corneum hydrated to 60% w/w differed from those at lower hydration levels: the scattering curve at 60% w/w showed only the diffraction peaks corresponding to a unit cell with a repeat distance of 6.4 nm. This observation implies that the ordering of a part of the lipids is reduced at very high water contents, which may explain the strong penetration-enhancing effects of water in the stratum corneum.

Crystallization↗