THE LIPID AND PROTEIN-STRUCTURE OF MOUSE STRATUM-CORNEUM - A WIDE AND SMALL-ANGLE DIFFRACTION STUDY
THE LIPID AND PROTEIN-STRUCTURE OF MOUSE STRATUM-CORNEUM - A WIDE AND SMALL-ANGLE DIFFRACTION STUDY
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DOI：
10.1016/0005-2760(94)90252-6
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发表时间：
1994-05-13
期刊：
影响因子：
--
通讯作者：
BRAS, W
中科院分区：
文献类型：
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作者：
BOUWSTRA, JA;GOORIS, GS;BRAS, W
用小角度和广角X射线散射法研究了小鼠角质层的结构。收集了作为温度和水合作用的函数的衍射图。脂质片层结构的重复距离为13.4 nm。偶尔还会发现重复距离为6.1 nm的第二类脂层状相。水化后未见板层肿胀，也未见脂肪侧方肿胀。在这些事实的基础上，得出结论：脂质结构的晶胞大小对水分不敏感。当加热到55℃时，13.4 nm的片层相消失，在45℃时，正交侧向堆积消失。在此温度下，只能观察到脂质的六角形和液体侧向堆积。在45℃~80℃之间，六方堆积转变为液体堆积，通过模型计算得到了层状结构的电子密度分布。在所有模型中，都拟合了三个电子透射区，其间有电子致密区，表明13.4 nm的层状结构由三个双层组成。
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.