## Abstract To investigate the influence of bleaching treatments on keratin fibers, the structure of crossβsections at various depths of bleached human hair (black and white human hair) was directly analyzed without isolating the cuticle and cortex, using Raman spectroscopy. The SβS band intensity
Reduction mechanism of L-cysteine on keratin fibers using microspectrophotometry and Raman spectroscopy
β Scribed by Akio Kuzuhara; Teruo Hori
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2005
- Tongue
- English
- Weight
- 372 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Abstract
In order to investigate the reduction mechanism of Lβcysteine (Cys) on keratin fibers, crossβsectional samples of virgin white human hair treated with Cys were prepared. The heterogeneous reaction between Cys and keratin fibers involving the diffusion of Cys into human hair was analyzed at the molecular level using microspectrophotometry and Raman spectroscopy. The diffusion pattern of Cys into human hair showed nonβFickian type characteristics, thus indicating the free amino groups of electrostatically interacted with the anionic ions of the fiber surface. The disconnected relative concentration of βSSβ groups at various depths of the hair samples with pH 9.0 was less than the Cys relative concentration, indicating that the reaction rate (the disconnection of βSSβ groups) was slower than the diffusion rate of Cys into human hair. From these experiments, we concluded that the free amino groups of Cys electrostatically interacted with the anionic ions of the fiber surface, thereby decreasing the reaction rate (the disconnection of βSSβ groups) of Cys at pH 9.0. Β© 2005 Wiley Periodicals, Inc. Biopolymers 79: 324β334, 2005
This article was originally published online as an accepted preprint. The βPublished Onlineβ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
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