Oriented structure in human stratum corneum revealed by X-ray diffraction

Abstract

Various types of human stratum corneum (sheets or callus) were exposed, in parallel and perpendicular geometry, to the high flux of X rays produced by a synchrotron radiation source. Under these conditions, very clear and rich diffraction patterns, corresponding to the supramolecular organization of stratum corneum proteins and lipids, were obtained. The comparative study of normal or delipidized stratum corneum sheets and membrane couplets allows one to attribute certain diffraction features to lipids. Our results in the 3-7nm range show two different distances for lipid bilayers. Concerning the protein nature of normal stratum corneum, the results show that keratin would occur in the β form, whereas for callus it is in the β form. Indeed, normal stratum corneum sheets never display the 0.514-nm characteristic of α keratin. This result means that the supramolecular organization of keratin could depend on the keratinization process. Finally, our studies also confirm the presence of a stillunknown protein component existing in the β form that would be located either inside the corneocytes or in some dilatated zones of the intercellular spaces. © 1991.