| Titre : |
Age-related hair denaturation related to protein carbonyls |
| Type de document : |
texte imprimé |
| Auteurs : |
Naoya Fuse, Auteur ; Shigeaki Morita, Auteur ; Yukako Matsue, Auteur |
| Année de publication : |
2024 |
| Article en page(s) : |
p. 348-356 |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Carbonylation
Cheveux -- Vieillissement
Chimie analytique
Dermatologie
Spectrométrie infrarouge
|
| Index. décimale : |
668.5 Parfums et cosmétiques |
| Résumé : |
- OBJECTIVE : Hair ageing is accompanied by hair fibres becoming irregularly shaped causing them to stick out in irregular directions or have more curliness and being spread out. This is believed to be due to changes within the hair fibre structure which occur with ageing, and one of the causes of these changes could be an increase in the number of protein carbonyl groups present in the hair. The aim of this study is to investigate the internal denaturation of hair related to protein carbonyls in attempt to gain new insight into age-related changes that occur in hair.
- METHODS : The degree of carbonylation of the hair structural protein as determined by fluorescent labelling and Western blotting analysis was used to investigate the primary structure of hair protein. The amount of helix, a common conformation in the secondary structure of proteins, in hair in groups of women with different ages was also analysed using infrared microscopy coupled with multivariate curve resolution (MCR). From the results of this, an image of the two-dimensional distribution of the α-helices was generated for the hair taken from each age group. Also, high-pressure differential scanning calorimetry (HPDSC) of the hair in water was performed on the hair taken from each age group to determine the peak temperature of endothermic effect and the enthalpy of denaturation.
- RESULTS : We found that the amino group content in hair proteins decreased and Type II keratin, one of the subunits of intermediate filament, was more carbonylated with age. The results of the MCR indicated eight separate components, including components of the secondary structure of proteins, such as α helices and β sheets. Two-dimensional images of the hair cross-sections revealed that the presence of α helices decreased with age. In addition, data from the HPDSC showed that the enthalpy associated with the denaturing temperature also significantly decreased with age.
- CONCLUSION : These results suggest that there is a negative correlation between age and structural integrity of the helix segment in intermediate filament. The results of this study also show that there is a positive correlation between age-related hair denaturation and protein carbonyls. |
| Note de contenu : |
- MATERIALS AND METHODS : Test material and chemicals - Measurement of average curvature of hair fibres - Visualization and quantification of amino groups in the hair - Western blot analysis - FT-IR microscopy analysis - High-pressure differential scanning calorimetry (HPDSC) - Statistical analysis
- RESULTS : Change of average curvature with age - Analysis of primary structure of hair protein-analysis of hair protein extract - Visualization of secondary structure of hair protein using FT-IR coupled MCR - Analysis of age-related denaturation of IF and IFAPs by HPDSC |
| DOI : |
https://doi.org/10.1111/ics.12934 |
| En ligne : |
https://drive.google.com/file/d/1qsAmxlVbPaHp3ixmrXw6vFgcPY9cyGPJ/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=41337 |
in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 46, N° 3 (06/2024) . - p. 348-356
Aller sur edunet
Accueil
Age-related hair denaturation related to protein carbonyls in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 46, N° 3 (06/2024)
