Abstract/3-Cyclodextrin-4-tert-butylbenzyl alcohol decahydrate, C42HvoO35

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 3-7-nm 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 beta form, whereas for callus it is in the alpha form. Indeed, normal stratum corneum sheets never display the 0.514-nm characteristic of alpha 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 still-unknown protein component existing in the beta form that would be located either inside the corneocytes or in some dilatated zones of the intercellular spaces.

Lead-based chemistry was initiated in ancient Egypt for cosmetic preparation more than 4000 years ago. Here, we study a hair-dyeing recipe using lead salts described in text since Greco-Roman times. We report direct evidence about the shape and distribution of PbS nanocrystals that form within the hair during blackening. It is remarkable that the composition and supramolecular organization of keratins can control PbS nanocrystal growth inside a hair.