Reduction mechanism of <scp>L</scp>‐cysteine on keratin fibers using microspectrophotometry and Raman spectroscopy

Kuzuhara, Akio; Hori, Teruo

doi:10.1002/bip.20362

Cited by 29 publications

(49 citation statements)

References 22 publications

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“…[48][49][50] This peak is absent in normal epidermis spectra, which reinforces the conclusion about the sensitivity of Episkin toward oxidative mechanisms.…”

Section: Figuresupporting

confidence: 83%

“…The same conclusion is given from the amide III band analysis (the peak at 1283 cm 21 (a helix) is more intense than the one at 1250 cm 21 (random coil)). 25,41,42,[47][48][49][50] Furthermore, the intense vibration at 935 cm 21 confirms the predominance of the a-helix conformation. These results agree with the previous studies about the evaluation of the secondary conformations of the epidermis.…”

Section: Proteins Of the Episkin Modelmentioning

confidence: 78%

“…These results agree with the previous studies about the evaluation of the secondary conformations of the epidermis. 25,29,[47][48][49][50][51] Lipids of the Episkin Model. The lipids of the epidermis are mainly constituted of ceramides, cholesterol, fatty acids, and membrane phospholipids of cells.…”

Section: Proteins Of the Episkin Modelmentioning

confidence: 99%

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Molecular characterization of reconstructed skin model by Raman microspectroscopy: Comparison with excised human skin

et al. 2007

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Human skin is directly exposed to different exogenous agents. Many research works have studied the diffusion, interactions, absorption mechanisms, and/or toxicity of these agents toward different cutaneous structures. With the use of living animals for such tests being more and more rejected; and the number of human volunteers being limited; different types of skin models are used. In the last few years, reconstructed epidermis from cell cultures has been frequently employed, and recent changes in the European chemical policy have approved and encouraged the use of these reconstructed models for skin‐related research works and assessments. Among the techniques used actually to study the skin, Raman microspectroscopy is a rising and powerful nondestructive technique that detects characteristic molecular vibrations. In this study, we created a spectral database to index the vibration peaks and bands of a well‐known reconstructed epidermis model, the Episkin®. The comparison with a native epidermis signal enabled us to put in evidence several spectral differences associated with molecular and structural differences between the skin and the reconstructed model, both maintained in living conditions. In addition to that, we have showed the feasibility of tracking the penetration of a pharmaceutical molecule through the Episkin model. © 2007 Wiley Periodicals, Inc. Biopolymers 87: 261–274, 2007.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…[48][49][50] This peak is absent in normal epidermis spectra, which reinforces the conclusion about the sensitivity of Episkin toward oxidative mechanisms.…”

Section: Figuresupporting

confidence: 83%

Section: Proteins Of the Episkin Modelmentioning

confidence: 78%

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Molecular characterization of reconstructed skin model by Raman microspectroscopy: Comparison with excised human skin

et al. 2007

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“…The direct characterization of keratin fibers has been performed using X-ray diffraction, 1,[7][8][9][10][11][12] solid state NMR, 8,13 Raman, [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] and Infrared spectroscopy. 14,16,17 Information about the amorphous region (the cuticle and matrix) of…”

Section: Introductionmentioning

confidence: 99%

“…On the other hand, when directly characterizing the cuticle and cortex structure of a single keratin fiber, the analytical technique using a Raman microscope is effective as it can be measured at a spot diameter of 1 lm. [20][21][22][23][24][25][26] Most importantly, by using this method, information about the crystalline fibrous (microfibril) and amorphous (matrix) structures existing in the cortex region can be obtained. However, up to now, Raman spectroscopic analysis had been limited to white human hair, [20][21][22][23][24][25][26] which has no melanin granules, and blond human hair, 27,28 which has few melanin granules.…”

Section: Introductionmentioning

confidence: 99%

Analysis of internal structure changes in black human hair keratin fibers with aging using Raman spectroscopy

Kuzuhara¹,

Fujiwara²,

Hori³

2007

Biopolymers

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To investigate the internal structure changes in virgin black human hair keratin fibers due to aging, the structure of cross‐sections at various depths of virgin black human hair (sections of new growth hair: 2 mm from the scalp) from a group of eight Japanese females in their twenties and another group of eight Japanese females in their fifties were analyzed using Raman spectroscopy. For the first time, we have succeeded in recording the Raman spectra of virgin black human hair, which had been impossible due to high melanin granule content. The key points of this method are to cross‐section hair samples to a thickness of 1.50‐μm, to select points at various depths of the cortex with the fewest possible melanin granules, and to optimize laser power, cross slit width as well as total acquisition time. The reproducibility of the Raman bands, namely the α‐helix (α) content, the β‐sheet and/or random coil (β/R) content, the disulfide (SS) content, and random coil content of two adjoining cross‐sections of a single hair keratin fiber was clearly good. The SS content of virgin black human hair from the Japanese females in their fifties for the cortex region decreased compared with that of the Japanese females in their twenties. On the other hand, the β/R and α contents of the cortex region did not change. © 2007 Wiley Periodicals, Inc. Biopolymers 87: 134–140, 2007.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Reinforced Wool Keratin Fibers via Dithiol Chain Re‐bonding

Zhu

et al. 2023

Adv Funct Materials

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Regenerated wool keratin fibers (RWKFs) have heretofore attracted tremendous interest according to environmental friendliness, ample resource, and intrinsic biocompatibility for broad applications. In this realm, both uncontrollable keratin fibril assembly procedure and resultant insufficient mechanical strength, have greatly hindered their large-scale manufacture and commercial viability. Herein, a continuous wet-spinning strategy is put forward to rebuild wool keratin into compact regenerated bio-fibers with improved strength via disulfide re-bonding. Dithiothreitol (DTT) has been introduced to renovate disulfide linkage inside keratin polypeptide chains, and bridge keratin fibrils via covalent thiol bonding to form a continuous backbone as mechanical support. A thus-derived RWKF manifests a tensile strength of 186.1 ± 7.0 MPa and Young's modulus of 7.4 ± 0.2 GPa, which exceeds those of natural wool, feathers, and regenerated wool or feather keratin fibers. The detailed wetspinning technical parameters, such as coagulation, oxidation, and posttreatment, have been systematically optimized to guarantee the continuous preparation of high-strength regenerated keratin fibers. This work offers insight into solving the concurrent challenges for continuous manufacture of regenerated protein fibers and sustainability concerns about biomass waste.

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Reduction mechanism of L‐cysteine on keratin fibers using microspectrophotometry and Raman spectroscopy

Cited by 29 publications

References 22 publications

Molecular characterization of reconstructed skin model by Raman microspectroscopy: Comparison with excised human skin

Molecular characterization of reconstructed skin model by Raman microspectroscopy: Comparison with excised human skin

Analysis of internal structure changes in black human hair keratin fibers with aging using Raman spectroscopy

Reinforced Wool Keratin Fibers via Dithiol Chain Re‐bonding

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