Investigating the relationship between changes in collagen fiber orientation during skin aging and collagen/water interactions by polarized-FTIR microimaging
| Autor: | Jean-François Angiboust, Michel Manfait, Marie-Danièle Diebold, Teddy Happillon, Christophe Eklouh-Molinier, Nicole Bouland, Sylvie Brassart-Pasco, Olivier Piot, Caroline Fichel |
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| Přispěvatelé: | Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS), Université de Reims Champagne-Ardenne (URCA), Plateforme en Imagerie Cellulaire et Tissulaire (PICT), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV) |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
In situ
Adult Collagen helix Human skin Nanotechnology Fibril Biochemistry Analytical Chemistry Skin Aging Spectroscopy Fourier Transform Infrared Electrochemistry Environmental Chemistry Bound water Humans Fourier transform infrared spectroscopy Deuterium Oxide Spectroscopy Aged Chemistry Water Middle Aged Molecular Imaging Biophysics [SPI.OPTI]Engineering Sciences [physics]/Optics / Photonic Female Collagen Type I collagen Algorithms |
| Zdroj: | Analyst Analyst, Royal Society of Chemistry, 2015, 140, pp.6260-6268. ⟨10.1039/c5an00278h⟩ |
| ISSN: | 0003-2654 1364-5528 |
| DOI: | 10.1039/c5an00278h⟩ |
| Popis: | International audience; Upon chronological aging, human skin undergoes structural and molecular modifications, especially at the level of type I collagen. This macromolecule is one of the main dermal structural proteins and presents several age-related alterations. It exhibits a triple helical structure and assembles itself to form fibrils and fibers. In addition, water plays an important role in stabilizing the collagen triple helix by forming hydrogen-bonds between collagen residues. However, the influence of water on changes of dermal collagen fiber orientation with age has not been yet understood. Polarized-Fourier Transform Infrared (P-FTIR) imaging is an interesting biophotonic approach to determine in situ the orientation of type I collagen fibers, as we have recently shown by comparing skin samples of different ages. In this work, P-FTIR spectral imaging was performed on skin samples from two age groups (35-and 38-year-old on the one hand, 60-and 66-year-old on the other hand), and our analyses were focused on the effect of H 2 O/D 2 O substitution. Spectral data were processed with fuzzy C-means (FCM) clustering in order to distinguish different orientations of collagen fibers. We demonstrated that the orientation was altered with aging, and that D 2 O treatment, affecting primarily highly bound water molecules, is more marked for the youngest skin samples. Collagen-bound water-related spectral markers were also highlighted. Our results suggest a weakening of water/collagen interactions with age. This non-destructive and label-free methodology allows us to understand better the importance of bound water in collagen fiber orientation alterations occurring with skin aging. Obtaining such structural information could find benefits in dermatology as well as in cosmetics. † Electronic supplementary information (ESI) available. See |
| Databáze: | OpenAIRE |
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